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Entry
Database: PDB / ID: 8gym
TitleCryo-EM structure of Tetrahymena thermophila respiratory mega-complex MC IV2+(I+III2+II)2
Components
  • (Acyl carrier ...) x 2
  • (Cytochrome c oxidase subunit ...) x 3
  • (Gamma-carbonic ...) x 2
  • (NADH dehydrogenase [ubiquinone] ...) x 8
  • (NADH dehydrogenase subunit ...) x 6
  • (NADH-ubiquinone oxidoreductase ...) x 7
  • (SURF1-like protein) x 2
  • (Succinate dehydrogenase ...) x 2
  • (Transmembrane ...) x 33
  • (Transposase) x 2
  • (Ubiquinol-cytochrome ...) x 2
  • (Unknown peptide) x 2
  • (Zf-Tim10_DDP domain-containing ...) x 2
  • 2 iron, 2 sulfur cluster-binding protein
  • 2-oxoglutarate/malate carrier protein
  • 37S ribosomal protein S25, mitochondrial
  • 39S ribosomal protein L9, mitochondrial
  • ABC transporter
  • ATP synthase subunit e, mitochondrial
  • Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II
  • Annexin
  • Apocytochrome b
  • CHCH domain-containing protein
  • COX assembly mitochondrial protein
  • COXTT10
  • COXTT22
  • COXTT28
  • COXTT3
  • COXTT9
  • CTF/NF-I domain-containing protein
  • CX9C domain-containing protein
  • Carrier protein
  • Chromosome condensation regulator RCC1 repeat protein
  • Complex I-MNLL
  • Complex III subunit VII
  • Cullin domain-containing protein
  • Cytochrome b-c1 complex subunit 8
  • Cytochrome protein c1
  • DUF4885 domain-containing protein
  • Decapping nuclease
  • Diphthamide synthesis protein
  • DnaJ domain protein
  • ETC complex I subunit motif protein
  • GRAM domain protein
  • Iron-binding zinc finger CDGSH type protein
  • Lipid-A-disaccharide synthase
  • Lysozyme
  • M16 family peptidase, putative
  • Mobilization protein
  • NAD-dependent epimerase/dehydratase family protein
  • NADH dehydrogenase, putative
  • NDUA13
  • NDUB10
  • NDUB2
  • NDUB4
  • NDUB6
  • NDUB8
  • NDUPH2
  • NDUTT15
  • NDUTT16
  • NDUTT17
  • NmrA domain-containing protein
  • Oxoglutarate/malate translocator protein, putative
  • PH domain-containing protein
  • Peptidase M16 inactive domain protein
  • Phage protein
  • Protein phosphatase 2C, putative
  • RNase III domain-containing protein
  • Ribosomal protein L51/S25/CI-B8 domain protein
  • Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
  • SDHD
  • SDHTT11
  • SDHTT3
  • Structural protein
  • Sulphotransf domain-containing protein
  • Thioredoxin
  • Tim10/DDP family zinc finger protein
  • TraB family protein
  • Transcription factor apfi protein, putative
  • UQCRTT2
  • YflT domain-containing protein
  • Ymf57
  • Ymf58
  • Ymf62
  • Ymf65
  • Ymf67
  • Ymf68
  • Ymf70
  • Ymf75
  • Zinc-finger protein
KeywordsELECTRON TRANSPORT / Electron transport chain / supercomplex / membrane protein / Tetrahymena thermophila
Function / homology
Function and homology information


dicarboxylic acid transmembrane transporter activity / lipid-A-disaccharide synthase / lipid-A-disaccharide synthase activity / NADH:ubiquinone reductase (H+-translocating) / quinol-cytochrome-c reductase / protein maturation by [2Fe-2S] cluster transfer / medium-chain fatty acid-CoA ligase activity / : / P450-containing electron transport chain / mitochondrial electron transport, succinate to ubiquinone ...dicarboxylic acid transmembrane transporter activity / lipid-A-disaccharide synthase / lipid-A-disaccharide synthase activity / NADH:ubiquinone reductase (H+-translocating) / quinol-cytochrome-c reductase / protein maturation by [2Fe-2S] cluster transfer / medium-chain fatty acid-CoA ligase activity / : / P450-containing electron transport chain / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase (quinone) activity / succinate dehydrogenase / NADH dehydrogenase complex / ubiquinone-6 biosynthetic process / : / : / oxidoreductase activity, acting on NAD(P)H / cytochrome-c oxidase / mitochondrial electron transport, cytochrome c to oxygen / 3 iron, 4 sulfur cluster binding / cytochrome-c oxidase activity / lipid A biosynthetic process / mitochondrial electron transport, ubiquinol to cytochrome c / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / quinone binding / : / tricarboxylic acid cycle / aerobic respiration / respiratory electron transport chain / fatty acid metabolic process / mitochondrial membrane / electron transport chain / phospholipid binding / 2 iron, 2 sulfur cluster binding / NAD binding / protein transport / FMN binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / electron transfer activity / oxidoreductase activity / ribosome / copper ion binding / DNA-binding transcription factor activity / heme binding / protein-containing complex binding / mitochondrion / membrane / nucleus / metal ion binding
Similarity search - Function
Surfeit locus 1/Shy1 / Surfeit locus 1/4 / TraB/PryY-like / SURF1 family / SURF1 family profile. / CTF transcription factor/nuclear factor 1, DNA-binding domain / CTF/NF-I DNA-binding domain profile. / Glycosyl transferase, family 19 / Lipid-A-disaccharide synthetase / : ...Surfeit locus 1/Shy1 / Surfeit locus 1/4 / TraB/PryY-like / SURF1 family / SURF1 family profile. / CTF transcription factor/nuclear factor 1, DNA-binding domain / CTF/NF-I DNA-binding domain profile. / Glycosyl transferase, family 19 / Lipid-A-disaccharide synthetase / : / : / Tim10-like / Tim10-like domain superfamily / : / Tim10/DDP family zinc finger / Mitochondrial substrate/solute carrier / Mitochondrial carrier domain superfamily / Mitochondrial carrier protein / Solute carrier (Solcar) repeat profile. / Iron-binding zinc finger, CDGSH type / MitoNEET, CDGSH iron-sulfur domain / CDGSH-type zinc finger. Function unknown. / Dynactin subunit 5 / : / : / : / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Succinate dehydrogenase, flavoprotein subunit / Adrenodoxin / : / Succinate dehydrogenase/fumarate reductase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, FAD-binding site / Fumarate reductase / succinate dehydrogenase FAD-binding site. / FAD-dependent oxidoreductase SdhA/FrdA/AprA / 4Fe-4S dicluster domain / Succinate dehydrogenase/fumarate reductase iron-sulphur protein / Succinate dehydogenase/fumarate reductase N-terminal / 2Fe-2S iron-sulfur cluster binding domain / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal / Fumarate reductase flavoprotein C-term / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily / FAD-dependent oxidoreductase 2, FAD binding domain / Alpha-helical ferredoxin / Cytochrome c oxidase subunit Vb, zinc binding region signature. / FAD binding domain / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / DnaJ domain / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c/quinol oxidase subunit II / : / DnaJ molecular chaperone homology domain / dnaJ domain profile. / 2Fe-2S ferredoxin, iron-sulphur binding site / 2Fe-2S ferredoxin-type iron-sulfur binding region signature. / Chaperone J-domain superfamily / DnaJ domain / Cytochrome c1 / Cytochrome C1 family / Hexapeptide repeat / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / 2Fe-2S iron-sulfur cluster binding domain / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome C oxidase subunit II, periplasmic domain / Rieske iron-sulphur protein, C-terminal / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Bacterial transferase hexapeptide (six repeats) / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / : / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain / Zinc finger, CHCC-type / Zinc-finger domain / Metalloenzyme, LuxS/M16 peptidase-like / Thioredoxin / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
Similarity search - Domain/homology
1,2-Distearoyl-sn-glycerophosphoethanolamine / ADENOSINE-5'-DIPHOSPHATE / CARDIOLIPIN / COPPER (II) ION / FE3-S4 CLUSTER / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C ...1,2-Distearoyl-sn-glycerophosphoethanolamine / ADENOSINE-5'-DIPHOSPHATE / CARDIOLIPIN / COPPER (II) ION / FE3-S4 CLUSTER / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-NDP / Chem-P5S / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE / IRON/SULFUR CLUSTER / Phosphatidylinositol / UBIQUINONE-10 / Chem-ZMP / Transmembrane protein, putative / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / Oxoglutarate/malate translocator protein, putative / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Transmembrane protein, putative / Transmembrane protein / SURF1-like protein / Uncharacterized protein / Uncharacterized protein / Diphthamide synthesis protein / Transmembrane protein / Transmembrane protein, putative / Uncharacterized protein / SURF1-like protein / Transmembrane protein / NADH dehydrogenase, putative / Transmembrane protein / succinate dehydrogenase / Transmembrane protein, putative / Gamma-carbonic anhydrase / Transmembrane protein / Iron-binding zinc finger CDGSH type protein / Transcription factor apfi protein, putative / Uncharacterized protein / Transmembrane protein, putative / Uncharacterized protein / Ribosomal protein L51/S25/CI-B8 domain protein / Transmembrane protein / Acyl carrier protein / Transmembrane protein / NADH-ubiquinone oxidoreductase 1, chain, putative / NADH-ubiquinone oxidoreductase 24 kDa subunit / Uncharacterized protein / Transmembrane protein, putative / Transmembrane protein / Transmembrane protein / Transmembrane protein, putative / Peptidase M16 inactive domain protein / Transmembrane protein, putative / Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit / Transmembrane protein / Uncharacterized protein / Transmembrane protein, putative / Uncharacterized protein / M16 family peptidase, putative / Zinc-finger protein / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / Transmembrane protein / NAD-dependent epimerase/dehydratase family protein / Transmembrane protein, putative / Transmembrane protein / NADH dehydrogenase subunit 1 / Uncharacterized protein / Thioredoxin / Ubiquinol-cytochrome C reductase hinge protein / CTF/NF-I domain-containing protein / Transmembrane protein, putative / Transmembrane protein, putative / DnaJ domain protein / lipid-A-disaccharide synthase / Transmembrane protein / Protein phosphatase 2C, putative / Transmembrane protein, putative / Transmembrane protein, putative / Uncharacterized protein / Transmembrane protein, putative / Transmembrane protein / Transmembrane protein, putative / 2 iron, 2 sulfur cluster-binding protein / Transmembrane protein, putative / Transmembrane protein / Acyl carrier protein / Gamma-carbonic anhydrase / Uncharacterized protein / Transmembrane protein, putative / Carrier protein / Uncharacterized protein / Tim10/DDP family zinc finger protein / Transmembrane protein / Uncharacterized protein / Uncharacterized protein
Similarity search - Component
Biological speciesTetrahymena thermophila SB210 (eukaryote)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.96 Å
AuthorsWu, M.C. / Hu, Y.Q. / Han, F.Z. / Zhou, L.
Funding support China, 1items
OrganizationGrant numberCountry
Other governmentZJU100 Young Professor China
CitationJournal: Nat Commun / Year: 2023
Title: Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae.
Authors: Fangzhu Han / Yiqi Hu / Mengchen Wu / Zhaoxiang He / Hongtao Tian / Long Zhou /
Abstract: Tetrahymena thermophila, a classic ciliate model organism, has been shown to possess tubular mitochondrial cristae and highly divergent electron transport chain involving four transmembrane protein ...Tetrahymena thermophila, a classic ciliate model organism, has been shown to possess tubular mitochondrial cristae and highly divergent electron transport chain involving four transmembrane protein complexes (I-IV). Here we report cryo-EM structures of its ~8 MDa megacomplex IV+ (I + III+ II), as well as a ~ 10.6 MDa megacomplex (IV + I + III+ II) at lower resolution. In megacomplex IV+ (I + III+ II), each CIV protomer associates one copy of supercomplex I + III and one copy of CII, forming a half ring-shaped architecture that adapts to the membrane curvature of mitochondrial cristae. Megacomplex (IV+ I + III+ II) defines the relative position between neighbouring half rings and maintains the proximity between CIV and CIII cytochrome c binding sites. Our findings expand the current understanding of divergence in eukaryotic electron transport chain organization and how it is related to mitochondrial morphology.
History
DepositionSep 23, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 14, 2023Provider: repository / Type: Initial release
Revision 1.1Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_admin / pdbx_entry_details / pdbx_modification_feature / pdbx_validate_chiral
Item: _em_admin.last_update / _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
1t: Tim10/DDP family zinc finger protein
2e: NmrA domain-containing protein
2f: Transmembrane protein, putative
2g: SDHTT3
2h: Diphthamide synthesis protein
2i: DUF4885 domain-containing protein
2j: Transmembrane protein, putative
2k: Transmembrane protein, putative
2l: Transposase
2m: Transmembrane protein, putative
2n: Transmembrane protein, putative
2o: SDHTT11
2t: Zf-Tim10_DDP domain-containing protein
3t: Zf-Tim10_DDP domain-containing protein
4a: Phage protein
4t: Transposase
5t: Cullin domain-containing protein
6a: Transmembrane protein, putative
6b: Structural protein
6c: Transmembrane protein, putative
6l: Decapping nuclease
6t: Annexin
7a: Transmembrane protein, putative
7c: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
7l: CTF/NF-I domain-containing protein
a: Transmembrane protein, putative
b: Protein phosphatase 2C, putative
bp: Chromosome condensation regulator RCC1 repeat protein
c1: Cytochrome c oxidase subunit 1
c2: Cytochrome c oxidase subunit 2
c3: Ymf68
d: SURF1-like protein
e: TraB family protein
f: Transmembrane protein, putative
fs: Iron-binding zinc finger CDGSH type protein
g: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8, mitochondrial
h: SURF1-like protein
i: COXTT9
j: COXTT10
k: 39S ribosomal protein L9, mitochondrial
l: Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C
m: Transmembrane protein, putative
m1: Oxoglutarate/malate translocator protein, putative
m2: 2-oxoglutarate/malate carrier protein
m3: Carrier protein
n: Transmembrane protein, putative
o: Mobilization protein
p: YflT domain-containing protein
q: Transmembrane protein, putative
r: Transmembrane protein
s: Complex III subunit VII
sa: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
sb: Succinate dehydrogenase (quinone)
sc: Cytochrome b-c1 complex subunit 8
sd: SDHD
t: Transmembrane protein, putative
u: Transmembrane protein, putative
v: COXTT22
vb: Cytochrome C oxidase subunit Vb protein
w: Transmembrane protein, putative
x: Transmembrane protein, putative
y: Lysozyme
y0: Ymf70
y5: Ymf75
y7: Ymf67
z: ABC transporter
z1: COXTT28
1b: NADH dehydrogenase subunit 1
2b: NADH dehydrogenase subunit 2
4l: Ymf58
5b: Ymf57
a1: Transmembrane protein, putative
a2: Ribosomal protein L51/S25/CI-B8 domain protein
a3: Transmembrane protein, putative
a5: ETC complex I subunit motif protein
a6: NADH dehydrogenase, putative
a7: 37S ribosomal protein S25, mitochondrial
a8: CX9C domain-containing protein
a9: NAD-dependent epimerase/dehydratase family protein
ab: Acyl carrier protein
ac: Acyl carrier protein
al: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
am: NDUA13
an: Transmembrane protein, putative
b2: NDUB2
b3: Transmembrane protein, putative
b4: NDUB4
b6: NDUB6
b7: CHCH domain-containing protein
b8: NDUB8
b9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
bl: NDUB10
bm: Transmembrane protein, putative
c4: Complex I-MNLL
fx: 2 iron, 2 sulfur cluster-binding protein
g1: Gamma-carbonic anhydrase
g2: Gamma-carbonic anhydrase
g3: Transcription factor apfi protein, putative
j1: DnaJ domain protein
n1: NADH-ubiquinone oxidoreductase chain 1
n2: Ymf65
n3: NADH-ubiquinone oxidoreductase chain 3
n4: NADH-ubiquinone oxidoreductase chain 4
n5: NADH dehydrogenase subunit 5
n6: Ymf62
p1: Transmembrane protein, putative
p2: NDUPH2
qA: M16 family peptidase, putative
qB: Peptidase M16 inactive domain protein
qC: Apocytochrome b
qD: Cytochrome protein c1
qE: Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
qF: Ubiquinol-cytochrome C reductase hinge protein
qG: Sulphotransf domain-containing protein
qH: Transmembrane protein, putative
qI: Transmembrane protein, putative
qJ: Transmembrane protein, putative
qL: UQCRTT2
qM: Unknown peptide
qa: M16 family peptidase, putative
qb: Peptidase M16 inactive domain protein
qc: Apocytochrome b
qd: Cytochrome protein c1
qe: Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
qf: Ubiquinol-cytochrome C reductase hinge protein
qg: Sulphotransf domain-containing protein
qh: Transmembrane protein, putative
qi: Transmembrane protein, putative
qj: Transmembrane protein, putative
ql: UQCRTT2
qm: Unknown peptide
s1: NADH-ubiquinone oxidoreductase 75 kDa subunit
s2: NADH dehydrogenase subunit 7
s3: NADH dehydrogenase subunit 9
s4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
s5: GRAM domain protein
s6: Zinc-finger protein
s7: NADH dehydrogenase subunit 10
s8: NADH-ubiquinone oxidoreductase 1, chain, putative
t1: Lipid-A-disaccharide synthase
t2: Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II
t3: RNase III domain-containing protein
t4: Transmembrane protein
t5: Transmembrane protein, putative
t6: COX assembly mitochondrial protein
t7: Transmembrane protein, putative
t8: PH domain-containing protein
t9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
ta: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
tb: Transmembrane protein, putative
tc: ATP synthase subunit e, mitochondrial
td: Transmembrane protein, putative
te: Transmembrane protein, putative
tf: NDUTT15
tg: NDUTT16
th: NDUTT17
tx: Thioredoxin
v1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
v2: NADH-ubiquinone oxidoreductase 24 kDa subunit
x1: NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit
1T: Tim10/DDP family zinc finger protein
2E: NmrA domain-containing protein
2F: Transmembrane protein, putative
2G: SDHTT3
2H: Diphthamide synthesis protein
2I: DUF4885 domain-containing protein
2J: Transmembrane protein, putative
2K: Transmembrane protein, putative
2L: Transposase
2M: Transmembrane protein, putative
2N: Transmembrane protein, putative
2O: SDHTT11
2T: Zf-Tim10_DDP domain-containing protein
3T: Zf-Tim10_DDP domain-containing protein
4A: Phage protein
4T: Transposase
5T: Cullin domain-containing protein
6A: Transmembrane protein, putative
6B: Structural protein
6C: Transmembrane protein, putative
6L: Decapping nuclease
6T: Annexin
7A: Transmembrane protein, putative
7C: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
7L: CTF/NF-I domain-containing protein
A: Transmembrane protein, putative
B: Protein phosphatase 2C, putative
BP: Chromosome condensation regulator RCC1 repeat protein
C1: Cytochrome c oxidase subunit 1
C2: Cytochrome c oxidase subunit 2
C3: Ymf68
D: SURF1-like protein
E: TraB family protein
F: Transmembrane protein, putative
FS: Iron-binding zinc finger CDGSH type protein
G: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8, mitochondrial
H: SURF1-like protein
I: COXTT9
J: COXTT10
K: 39S ribosomal protein L9, mitochondrial
L: Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C
M: Transmembrane protein, putative
M1: Oxoglutarate/malate translocator protein, putative
M2: 2-oxoglutarate/malate carrier protein
M3: Carrier protein
N: Transmembrane protein, putative
O: Mobilization protein
P: YflT domain-containing protein
Q: Transmembrane protein, putative
R: Transmembrane protein
S: Complex III subunit VII
SA: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
SB: Succinate dehydrogenase (quinone)
SC: Cytochrome b-c1 complex subunit 8
SD: SDHD
T: Transmembrane protein, putative
U: Transmembrane protein, putative
V: COXTT22
VB: Cytochrome C oxidase subunit Vb protein
W: Transmembrane protein, putative
X: Transmembrane protein, putative
Y: Lysozyme
Y0: Ymf70
Y5: Ymf75
Y7: Ymf67
Z: ABC transporter
Z1: COXTT28
1B: NADH dehydrogenase subunit 1
2B: NADH dehydrogenase subunit 2
4L: Ymf58
5B: Ymf57
A1: Transmembrane protein, putative
A2: Ribosomal protein L51/S25/CI-B8 domain protein
A3: Transmembrane protein, putative
A5: ETC complex I subunit motif protein
A6: NADH dehydrogenase, putative
A7: 37S ribosomal protein S25, mitochondrial
A8: CX9C domain-containing protein
A9: NAD-dependent epimerase/dehydratase family protein
AB: Acyl carrier protein
AC: Acyl carrier protein
AL: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
AM: NDUA13
AN: Transmembrane protein, putative
B2: NDUB2
B3: Transmembrane protein, putative
B4: NDUB4
B6: NDUB6
B7: CHCH domain-containing protein
B8: NDUB8
B9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
BL: NDUB10
BM: Transmembrane protein, putative
C4: Complex I-MNLL
FX: 2 iron, 2 sulfur cluster-binding protein
G1: Gamma-carbonic anhydrase
G2: Gamma-carbonic anhydrase
G3: Transcription factor apfi protein, putative
J1: DnaJ domain protein
N1: NADH-ubiquinone oxidoreductase chain 1
N2: Ymf65
N3: NADH-ubiquinone oxidoreductase chain 3
N4: NADH-ubiquinone oxidoreductase chain 4
N5: NADH dehydrogenase subunit 5
N6: Ymf62
P1: Transmembrane protein, putative
P2: NDUPH2
QA: M16 family peptidase, putative
QB: Peptidase M16 inactive domain protein
QC: Apocytochrome b
QD: Cytochrome protein c1
QE: Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
QF: Ubiquinol-cytochrome C reductase hinge protein
QG: Sulphotransf domain-containing protein
QH: Transmembrane protein, putative
QI: Transmembrane protein, putative
QJ: Transmembrane protein, putative
QL: UQCRTT2
Qa: M16 family peptidase, putative
Qb: Peptidase M16 inactive domain protein
Qc: Apocytochrome b
Qd: Cytochrome protein c1
Qe: Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
Qf: Ubiquinol-cytochrome C reductase hinge protein
Qg: Sulphotransf domain-containing protein
Qh: Transmembrane protein, putative
Qi: Transmembrane protein, putative
Qj: Transmembrane protein, putative
Ql: UQCRTT2
Qm: Unknown peptide
S1: NADH-ubiquinone oxidoreductase 75 kDa subunit
S2: NADH dehydrogenase subunit 7
S3: NADH dehydrogenase subunit 9
S4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
S5: GRAM domain protein
S6: Zinc-finger protein
S7: NADH dehydrogenase subunit 10
S8: NADH-ubiquinone oxidoreductase 1, chain, putative
T1: Lipid-A-disaccharide synthase
T2: Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II
T3: RNase III domain-containing protein
T4: Transmembrane protein
T5: Transmembrane protein, putative
T6: COX assembly mitochondrial protein
T7: Transmembrane protein, putative
T8: PH domain-containing protein
T9: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
TA: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
TB: Transmembrane protein, putative
TC: ATP synthase subunit e, mitochondrial
TD: Transmembrane protein, putative
TE: Transmembrane protein, putative
TF: NDUTT15
TG: NDUTT16
TH: NDUTT17
TX: Thioredoxin
V1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
V2: NADH-ubiquinone oxidoreductase 24 kDa subunit
X1: NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit
C: COXTT3
c: COXTT3
u1: Unknown peptide
u2: Unknown peptide
U2: Unknown peptide
QM: Unknown peptide
U1: Unknown peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,057,423836
Polymers8,555,282326
Non-polymers502,142510
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 79 types, 170 molecules 1t1T2e2E2g2G2h2H2i2I2l2L4a4A4t4T5t5T6b6B6l6L6t6T7l7LbBbpBP...

#1: Protein Tim10/DDP family zinc finger protein


Mass: 8008.990 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7X3D6
#2: Protein NmrA domain-containing protein


Mass: 36376.008 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24I09
#4: Protein SDHTT3


Mass: 23627.730 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MEX7
#5: Protein Diphthamide synthesis protein


Mass: 22894.336 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LX66
#6: Protein DUF4885 domain-containing protein


Mass: 12979.428 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22YL0
#9: Protein Transposase


Mass: 11027.419 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7XBF5
#15: Protein Phage protein


Mass: 14740.897 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24C97
#16: Protein Transposase


Mass: 8081.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22A35
#17: Protein Cullin domain-containing protein


Mass: 8965.917 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22N23
#19: Protein Structural protein


Mass: 27946.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24I72
#21: Protein Decapping nuclease


Mass: 10200.682 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LVX0
#22: Protein Annexin


Mass: 8155.360 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q233U0
#25: Protein CTF/NF-I domain-containing protein


Mass: 116812.750 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22CI1
#27: Protein Protein phosphatase 2C, putative


Mass: 53011.297 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22FX8
#28: Protein Chromosome condensation regulator RCC1 repeat protein


Mass: 50912.336 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#31: Protein Ymf68


Mass: 72782.539 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y6
#32: Protein SURF1-like protein


Mass: 47087.973 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M1Q4
#33: Protein TraB family protein


Mass: 45022.914 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23DP7
#35: Protein Iron-binding zinc finger CDGSH type protein


Mass: 21476.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M8P0
#37: Protein SURF1-like protein


Mass: 35794.367 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LTZ4
#38: Protein COXTT9


Mass: 29865.686 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LY65
#39: Protein COXTT10


Mass: 28101.486 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MD70
#40: Protein 39S ribosomal protein L9, mitochondrial


Mass: 27034.711 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7X4J9
#43: Protein Oxoglutarate/malate translocator protein, putative


Mass: 40392.234 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: A4VDV3
#44: Protein 2-oxoglutarate/malate carrier protein


Mass: 36090.277 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23M99
#45: Protein Carrier protein


Mass: 37095.141 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22ZA6
#47: Protein Mobilization protein


Mass: 23257.660 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23F08
#48: Protein YflT domain-containing protein


Mass: 19979.320 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M8Y9
#51: Protein Complex III subunit VII


Mass: 19882.758 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q230X6
#54: Protein Cytochrome b-c1 complex subunit 8


Mass: 7036.020 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23RH8
#58: Protein COXTT22


Mass: 17701.115 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MFV5
#62: Protein Lysozyme


Mass: 12273.913 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M9E7
#63: Protein Ymf70


Mass: 10891.920 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y0
#64: Protein Ymf75


Mass: 23325.801 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q951A7
#65: Protein Ymf67


Mass: 54538.531 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y7
#66: Protein ABC transporter


Mass: 10418.697 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LTF1
#67: Protein COXTT28


Mass: 11121.555 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#70: Protein Ymf58


Mass: 13509.949 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Z5
#71: Protein Ymf57


Mass: 12473.938 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q951C2
#73: Protein Ribosomal protein L51/S25/CI-B8 domain protein


Mass: 12157.782 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MA77
#75: Protein ETC complex I subunit motif protein


Mass: 24277.859 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23ND5
#76: Protein NADH dehydrogenase, putative


Mass: 20167.854 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M2Y3
#77: Protein 37S ribosomal protein S25, mitochondrial


Mass: 33201.797 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MIJ7
#78: Protein CX9C domain-containing protein


Mass: 28412.805 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MMF4
#79: Protein NAD-dependent epimerase/dehydratase family protein


Mass: 41375.090 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MLH2
#83: Protein NDUA13


Mass: 21045.617 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M2U4
#85: Protein NDUB2


Mass: 14410.395 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MG29
#87: Protein NDUB4


Mass: 17502.564 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#88: Protein NDUB6


Mass: 15444.344 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q231G0
#89: Protein CHCH domain-containing protein


Mass: 13747.362 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MIM0
#90: Protein NDUB8


Mass: 24150.469 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M855
#92: Protein NDUB10


Mass: 22167.137 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23KG0
#94: Protein Complex I-MNLL


Mass: 12103.036 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22W63
#95: Protein 2 iron, 2 sulfur cluster-binding protein


Mass: 19564.221 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22W11
#98: Protein Transcription factor apfi protein, putative


Mass: 39793.414 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M8Q7
#99: Protein DnaJ domain protein


Mass: 36878.367 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22DR7
#101: Protein Ymf65


Mass: 43104.082 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q951A3
#105: Protein Ymf62


Mass: 30448.471 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y2
#107: Protein NDUPH2


Mass: 22446.637 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23KE0
#108: Protein
M16 family peptidase, putative


Mass: 53030.543 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MJ25
#109: Protein
Peptidase M16 inactive domain protein


Mass: 58023.914 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MGU2
#110: Protein
Apocytochrome b


Mass: 50635.547 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Z1, quinol-cytochrome-c reductase
#111: Protein
Cytochrome protein c1


Mass: 37616.629 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24IM5
#112: Protein
Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit


Mass: 30696.961 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MIC7
#114: Protein
Sulphotransf domain-containing protein


Mass: 39193.523 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23F81
#124: Protein GRAM domain protein


Mass: 10920.431 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7X4R4
#125: Protein Zinc-finger protein


Mass: 15141.296 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MK02
#128: Protein Lipid-A-disaccharide synthase


Mass: 59307.289 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22E24, lipid-A-disaccharide synthase
#129: Protein Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II


Mass: 36709.441 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24HK5
#130: Protein RNase III domain-containing protein


Mass: 35409.246 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: I7LUQ4
#133: Protein COX assembly mitochondrial protein


Mass: 17078.342 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M1N8
#135: Protein PH domain-containing protein


Mass: 15785.234 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22SC4
#139: Protein ATP synthase subunit e, mitochondrial


Mass: 11283.534 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22E95
#142: Protein NDUTT15


Mass: 27562.686 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#143: Protein NDUTT16


Mass: 15465.568 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#144: Protein NDUTT17


Mass: 14124.288 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
#145: Protein Thioredoxin


Mass: 19540.191 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22AI5
#149: Protein COXTT3


Mass: 23368.416 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#150: Protein Unknown peptide


Mass: 7847.665 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences

+
Transmembrane ... , 33 types, 72 molecules 2f2F2j2J2k2K2m2M2n2N6a6A6c6C7a7AaAfFmMnNqQrRtT...

#3: Protein Transmembrane protein, putative


Mass: 35124.293 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q248F8
#7: Protein Transmembrane protein, putative


Mass: 11957.518 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23S01
#8: Protein Transmembrane protein, putative


Mass: 11188.824 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24CW6
#10: Protein Transmembrane protein, putative


Mass: 9168.366 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22HD6
#11: Protein Transmembrane protein, putative


Mass: 7244.434 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7XF00
#18: Protein Transmembrane protein, putative


Mass: 15618.258 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7XCY5
#20: Protein Transmembrane protein, putative


Mass: 12786.321 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23DS4
#23: Protein Transmembrane protein, putative


Mass: 16385.635 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MGF9
#26: Protein Transmembrane protein, putative


Mass: 57814.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22PJ5
#34: Protein Transmembrane protein, putative


Mass: 41307.387 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23DG8
#42: Protein Transmembrane protein, putative


Mass: 26601.174 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7WZP1
#46: Protein Transmembrane protein, putative


Mass: 24701.131 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LZX8
#49: Protein Transmembrane protein, putative


Mass: 20346.227 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23D87
#50: Protein Transmembrane protein


Mass: 20025.109 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MKT6
#56: Protein Transmembrane protein, putative


Mass: 18801.604 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23VY4
#57: Protein Transmembrane protein, putative


Mass: 18600.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22DP8
#60: Protein Transmembrane protein, putative


Mass: 15588.598 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23TE5
#61: Protein Transmembrane protein, putative


Mass: 14302.487 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22W32
#72: Protein Transmembrane protein, putative


Mass: 11451.183 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MI60
#74: Protein Transmembrane protein, putative


Mass: 15831.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M9B3
#84: Protein Transmembrane protein, putative


Mass: 26545.146 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24F24
#86: Protein Transmembrane protein, putative


Mass: 9942.366 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: A4VD20
#93: Protein Transmembrane protein, putative


Mass: 24419.150 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22Z32
#106: Protein Transmembrane protein, putative


Mass: 29389.660 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q24C39
#115: Protein
Transmembrane protein, putative


Mass: 15677.771 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M484
#116: Protein
Transmembrane protein, putative


Mass: 14262.554 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MM45
#117: Protein
Transmembrane protein, putative


Mass: 7455.741 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MFL6
#131: Protein Transmembrane protein


Mass: 24823.297 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MIE0
#132: Protein Transmembrane protein, putative


Mass: 23971.033 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LT77
#134: Protein Transmembrane protein, putative


Mass: 16909.242 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22HE4
#138: Protein Transmembrane protein, putative


Mass: 13340.979 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22T55
#140: Protein Transmembrane protein, putative


Mass: 8787.116 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22DC2
#141: Protein Transmembrane protein, putative


Mass: 8445.937 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MIK1

+
Protein/peptide , 4 types, 14 molecules 2o2OsdSDqLqlQLQlqMqmQmu2U2QM

#12: Protein/peptide SDHTT11


Mass: 5459.540 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#55: Protein/peptide SDHD


Mass: 5553.692 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#118: Protein/peptide
UQCRTT2


Mass: 4850.612 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
#119: Protein/peptide
Unknown peptide


Mass: 1464.797 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences

+
Zf-Tim10 DDP domain-containing ... , 2 types, 4 molecules 2t2T3t3T

#13: Protein Zf-Tim10_DDP domain-containing protein


Mass: 8354.574 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7XDM6
#14: Protein Zf-Tim10_DDP domain-containing protein


Mass: 10435.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q231A8

+
NADH dehydrogenase [ubiquinone] ... , 8 types, 16 molecules 7c7CgGalALb9B9s4S4t9T9taTAv1V1

#24: Protein NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial


Mass: 28666.662 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: W7X287
#36: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8, mitochondrial


Mass: 37552.980 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23DZ5
#82: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12


Mass: 22890.570 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: A4VDQ6
#91: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial


Mass: 22698.301 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q233X7
#123: Protein NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial


Mass: 21642.377 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MK61
#136: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8


Mass: 15689.792 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23B10
#137: Protein NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4


Mass: 15193.583 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MAF0
#146: Protein NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial


Mass: 52313.699 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23KE4, NADH:ubiquinone reductase (H+-translocating)

+
Cytochrome c oxidase subunit ... , 3 types, 6 molecules c1C1c2C2vbVB

#29: Protein Cytochrome c oxidase subunit 1


Mass: 80564.945 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y4, cytochrome-c oxidase
#30: Protein Cytochrome c oxidase subunit 2


Mass: 72388.883 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y9, cytochrome-c oxidase
#59: Protein Cytochrome C oxidase subunit Vb protein


Mass: 75431.312 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23FF5

+
Ubiquinol-cytochrome ... , 2 types, 6 molecules lLqFqfQFQf

#41: Protein Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C


Mass: 26738.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M3P9
#113: Protein
Ubiquinol-cytochrome C reductase hinge protein


Mass: 10249.956 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22AX2

+
Succinate dehydrogenase ... , 2 types, 4 molecules saSAsbSB

#52: Protein Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial


Mass: 70082.758 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23DI3
#53: Protein Succinate dehydrogenase (quinone) / Iron-sulfur subunit of complex II


Mass: 36002.402 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M403, succinate dehydrogenase

+
NADH dehydrogenase subunit ... , 6 types, 12 molecules 1b1B2b2Bn5N5s2S2s3S3s7S7

#68: Protein NADH dehydrogenase subunit 1


Mass: 7238.754 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q09FB0
#69: Protein NADH dehydrogenase subunit 2


Mass: 20899.889 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q951B2, NADH:ubiquinone reductase (H+-translocating)
#104: Protein NADH dehydrogenase subunit 5


Mass: 88179.844 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Z0, NADH:ubiquinone reductase (H+-translocating)
#121: Protein NADH dehydrogenase subunit 7


Mass: 51227.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q951B1, NADH:ubiquinone reductase (H+-translocating)
#122: Protein NADH dehydrogenase subunit 9


Mass: 23803.268 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Z4, NADH:ubiquinone reductase (H+-translocating)
#126: Protein NADH dehydrogenase subunit 10


Mass: 18324.260 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q951B4, NADH:ubiquinone reductase (H+-translocating)

+
Acyl carrier ... , 2 types, 4 molecules abABacAC

#80: Protein Acyl carrier protein


Mass: 16249.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22XT6
#81: Protein Acyl carrier protein


Mass: 15428.433 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MD12

+
Gamma-carbonic ... , 2 types, 4 molecules g1G1g2G2

#96: Protein Gamma-carbonic anhydrase


Mass: 28216.734 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q22XU5
#97: Protein Gamma-carbonic anhydrase


Mass: 25395.969 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7M6S0

+
NADH-ubiquinone oxidoreductase ... , 7 types, 14 molecules n1N1n3N3n4N4s1S1s8S8v2V2x1X1

#100: Protein NADH-ubiquinone oxidoreductase chain 1


Mass: 32636.770 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Y3, NADH:ubiquinone reductase (H+-translocating)
#102: Protein NADH-ubiquinone oxidoreductase chain 3


Mass: 14416.898 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950Z7, NADH:ubiquinone reductase (H+-translocating)
#103: Protein NADH-ubiquinone oxidoreductase chain 4


Mass: 58690.043 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q950X9, NADH:ubiquinone reductase (H+-translocating)
#120: Protein NADH-ubiquinone oxidoreductase 75 kDa subunit


Mass: 80580.789 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: Q23KA9
#127: Protein NADH-ubiquinone oxidoreductase 1, chain, putative


Mass: 28053.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MDW5
#147: Protein NADH-ubiquinone oxidoreductase 24 kDa subunit


Mass: 31216.697 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7MEP0
#148: Protein NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit


Mass: 17381.809 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote)
Plasmid details: Institute of Hydrobiology, Chinese Academy of Sciences
References: UniProt: I7LT42

+
Non-polymers , 21 types, 510 molecules

#151: Chemical
ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C34H34FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#152: Chemical...
ChemComp-PC1 / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 3-SN-PHOSPHATIDYLCHOLINE


Mass: 790.145 Da / Num. of mol.: 168 / Source method: obtained synthetically / Formula: C44H88NO8P / Comment: phospholipid*YM
#153: Chemical...
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL


Mass: 1464.043 Da / Num. of mol.: 198 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#154: Chemical
ChemComp-HEA / HEME-A


Mass: 852.837 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C49H56FeN4O6 / Feature type: SUBJECT OF INVESTIGATION
#155: Chemical
ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cu / Feature type: SUBJECT OF INVESTIGATION
#156: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#157: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Fe2S2 / Feature type: SUBJECT OF INVESTIGATION
#158: Chemical...
ChemComp-3PE / 1,2-Distearoyl-sn-glycerophosphoethanolamine / 3-SN-PHOSPHATIDYLETHANOLAMINE / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE


Mass: 748.065 Da / Num. of mol.: 48 / Source method: obtained synthetically / Formula: C41H82NO8P / Comment: phospholipid*YM
#159: Chemical ChemComp-P5S / O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine / phosphatidyl serine


Mass: 792.075 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C42H82NO10P
#160: Chemical
ChemComp-PX2 / 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE


Mass: 535.671 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C27H52O8P
#161: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
#162: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: Fe4S4
#163: Chemical ChemComp-F3S / FE3-S4 CLUSTER


Mass: 295.795 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe3S4
#164: Chemical
ChemComp-U10 / UBIQUINONE-10 / Coenzyme Q10


Mass: 863.343 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C59H90O4 / Feature type: SUBJECT OF INVESTIGATION
#165: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#166: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#167: Chemical ChemComp-NDP / NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE


Mass: 745.421 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H30N7O17P3
#168: Chemical ChemComp-ZMP / S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate


Mass: 568.704 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C25H49N2O8PS / Feature type: SUBJECT OF INVESTIGATION
#169: Chemical ChemComp-T7X / Phosphatidylinositol


Mass: 887.128 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C47H83O13P
#170: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#171: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE


Mass: 456.344 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H21N4O9P / Feature type: SUBJECT OF INVESTIGATION

+
Details

Has ligand of interestY
Has protein modificationY

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Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: Tetrahymena thermophila respiratory mega-complex MC (IV2+I+III2+II)2
Type: COMPLEX / Entity ID: #1-#150 / Source: NATURAL
Molecular weightValue: 8 MDa / Experimental value: NO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Buffer solutionpH: 7.4
Details: SEC buffer (20 mM Tris pH 7.4, 50 mM NaCl, 0.002% PMSF, 0.005% LMNG (w/v))
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMTrimethylsilylTris1
250 mMSodium chlorideNaCl1
30.002 %Phenylmethylsulfonyl fluoridePMSF1
40.005 %lauryl maltose neopentyl glycolLMNG1
SpecimenConc.: 4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: 25 mA / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 140000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 7 sec. / Electron dose: 61.5 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 16772
Image scansWidth: 4096 / Height: 4096

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Processing

Software
NameVersionClassificationNB
phenix.real_space_refine1.20.1_4487refinement
PHENIX1.20.1_4487refinement
EM software
IDNameVersionCategory
1crYOLO1.6.0particle selection
2EPUimage acquisition
4CTFFIND4.1CTF correction
7PHENIX1.20.1model fitting
8Coot0.9.6model fitting
10cryoSPARCv3.3.2initial Euler assignment
11cryoSPARCv3.3.2final Euler assignment
12cryoSPARCv3.3.2classification
13cryoSPARCv3.3.23D reconstruction
14PHENIX1.20.1model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1220892
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 2.96 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 97688 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 56.79 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0022582734
ELECTRON MICROSCOPYf_angle_d0.4561785758
ELECTRON MICROSCOPYf_chiral_restr0.039581536
ELECTRON MICROSCOPYf_plane_restr0.003598122
ELECTRON MICROSCOPYf_dihedral_angle_d11.1596223300

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Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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