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- PDB-9f5x: Structure of the Chlamydomonas reinhardtii respiratory supercompl... -

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Basic information

Entry
Database: PDB / ID: 9f5x
TitleStructure of the Chlamydomonas reinhardtii respiratory supercomplex I1 III2 IV2
Components
  • (Cytochrome b-c1 complex subunit ...) x 3
  • (Cytochrome c oxidase ...) x 4
  • (Mitochondrial NADH:ubiquinone oxidoreductase ...) x 9
  • (Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit ...) x 2
  • (NADH dehydrogenase [ubiquinone] ...) x 6
  • (NADH-ubiquinone oxidoreductase chain ...) x 6
  • (NADH:ubiquinone oxidoreductase ...) x 11
  • (Putative NADH:ubiquinone oxidoreductase ...) x 3
  • AGGG
  • ASHI
  • Acyl carrier protein
  • Alpha-MPP
  • B14.5a
  • B9
  • CAG1
  • CAG2 - CA-like
  • Complex III subunit 9
  • Cox5b
  • Cox5c
  • Cox6a
  • Cox6b
  • Cox7a
  • Cox7c
  • CoxIn
  • Cytochrome b
  • Cytochrome c1
  • ESSS
  • KFYI
  • MPP-Beta
  • Mitochondrial putative NADH:ubiquinone oxidoreductase 6.5 kDa subunit
  • NADH dehydrogenase subunit 4L
  • NUOP7
  • NUOP8
  • P10
  • P9
  • cytochrome-c oxidase
KeywordsMEMBRANE PROTEIN / Mitochondria / respiratory complex / respiration / alga
Function / homology
Function and homology information


NADH:ubiquinone reductase (H+-translocating) / TIM22 mitochondrial import inner membrane insertion complex / NADH dehydrogenase / quinol-cytochrome-c reductase / mitochondrion targeting sequence binding / protein insertion into mitochondrial inner membrane / NADH dehydrogenase complex / ubiquinone biosynthetic process / respiratory chain complex IV / mitochondrial envelope ...NADH:ubiquinone reductase (H+-translocating) / TIM22 mitochondrial import inner membrane insertion complex / NADH dehydrogenase / quinol-cytochrome-c reductase / mitochondrion targeting sequence binding / protein insertion into mitochondrial inner membrane / NADH dehydrogenase complex / ubiquinone biosynthetic process / respiratory chain complex IV / mitochondrial envelope / cytochrome-c oxidase / respiratory chain complex III / oxidative phosphorylation / quinol-cytochrome-c reductase / oxidoreductase activity, acting on NAD(P)H / mitochondrial electron transport, cytochrome c to oxygen / quinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / acyl binding / acyl carrier activity / electron transport coupled proton transport / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / phosphopantetheine binding / protein transmembrane transporter activity / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / proton transmembrane transport / aerobic respiration / respiratory electron transport chain / electron transport chain / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / metallopeptidase activity / FMN binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / mitochondrial inner membrane / oxidoreductase activity / copper ion binding / heme binding / protein-containing complex binding / mitochondrion / metal ion binding / membrane
Similarity search - Function
Mitochondrial import inner membrane translocase subunit TIM22 / Putative NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / : / : / : / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Cytochrome c oxidase, subunit VIb ...Mitochondrial import inner membrane translocase subunit TIM22 / Putative NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / : / : / : / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Cytochrome c oxidase, subunit VIb / : / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome b-c1 complex, subunit 6 / Cytochrome c oxidase subunit I domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Cytochrome c/quinol oxidase subunit II / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome c1, transmembrane anchor, C-terminal / : / Cytochrome b / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Hexapeptide repeat / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / : / Cytochrome c1 / Cytochrome C1 family / 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. / : / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome C oxidase subunit II, periplasmic domain / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Tim17/Tim22/Tim23/Pmp24 family / Rieske iron-sulphur protein, C-terminal / Bacterial transferase hexapeptide (six repeats) / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / : / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / Metalloenzyme, LuxS/M16 peptidase-like / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / GRIM-19 / GRIM-19 protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NDUFB9, LYR domain / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / 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 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / ETC complex I subunit conserved region
Similarity search - Domain/homology
1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / Chem-8Q1 / CARDIOLIPIN / CROTONYL COENZYME A / COPPER (II) ION / DINUCLEAR COPPER ION / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C ...1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / Chem-8Q1 / CARDIOLIPIN / CROTONYL COENZYME A / COPPER (II) ION / DINUCLEAR COPPER ION / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-NDP / Chem-PC7 / Chem-PGT / PHOSPHATIDYLETHANOLAMINE / IRON/SULFUR CLUSTER / Chem-UQ5 / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Cytochrome b-c1 complex subunit 7 / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH:ubiquinone oxidoreductase 30kDa subunit domain-containing protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10 / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8 / Uncharacterized protein / Uncharacterized protein / Cytochrome b-c1 complex subunit 6 / Uncharacterized protein / Complex III subunit 9 / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Cytochrome c oxidase subunit 1 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 6 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 4 / Cytochrome b / Mitochondrial NADH:ubiquinone oxidoreductase 16 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 19 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 10 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 23 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 9 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 7.5 kDa subunit / Mitochondrial putative NADH:ubiquinone oxidoreductase 6.5 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 13 kDa subunit / Mitochondrial NADH:ubiquinone oxidoreductase 32 kDa subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / Mitochondrial NADH:ubiquinone oxidoreductase 18 kDa subunit / Acyl carrier protein / NADH:ubiquinone oxidoreductase 78 kDa subunit / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH:ubiquinone oxidoreductase B14 subunit / NADH:ubiquinone oxidoreductase 20,9 kD-like subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH:ubiquinone oxidoreductase 13 kD-like subunit / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH-ubiquinone oxidoreductase chain 3 / Putative NADH:ubiquinone oxidoreductase 12.5 kDa subunit / Putative NADH:ubiquinone oxidoreductase 17.8 kDa subunit / Putative NADH:ubiquinone oxidoreductase 39 kDa subunit / NADH:ubiquinone oxidoreductase 49 kD subunit / NADH:ubiquinone oxidoreductase B8 subunit / NADH:ubiquinone oxidoreductase subunit 10 / NADH:ubiquinone oxidoreductase subunit 8 / NADH:ubiquinone oxidoreductase 24 kD subunit / NADH dehydrogenase subunit 4L / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome c oxidase subunit / cytochrome-c oxidase / Cytochrome c oxidase polypeptide II / Cytochrome c1 / Cytochrome c oxidase subunit 3
Similarity search - Component
Biological speciesChlamydomonas reinhardtii (plant)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.82 Å
AuthorsWaltz, F. / Righetto, R. / Kotecha, A. / Engel, B.D.
Funding support Germany, Switzerland, 2items
OrganizationGrant numberCountry
Alexander von Humboldt Foundation Germany
Swiss National Science Foundation210561 Switzerland
CitationJournal: Science / Year: 2025
Title: In-cell architecture of the mitochondrial respiratory chain.
Authors: Florent Waltz / Ricardo D Righetto / Lorenz Lamm / Thalia Salinas-Giegé / Ron Kelley / Xianjun Zhang / Martin Obr / Sagar Khavnekar / Abhay Kotecha / Benjamin D Engel /
Abstract: Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, ...Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, working in concert to transfer electrons and pump protons. The precise organization of these complexes in native cells is debated. We used in situ cryo-electron tomography to visualize the native structures and organization of several major mitochondrial complexes in cells. ATP synthases and respiratory complexes segregate into curved and flat crista membrane domains, respectively. Respiratory complexes I, III, and IV assemble into a respirasome supercomplex, from which we determined a native 5-angstrom (Å) resolution structure showing binding of electron carrier cytochrome . Combined with single-particle cryo-electron microscopy at 2.4-Å resolution, we model how the respiratory complexes organize inside native mitochondria.
History
DepositionApr 30, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 12, 2025Provider: repository / Type: Initial release
Revision 1.0Mar 12, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Mar 12, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
1A: Cytochrome b
1B: Cytochrome b
1C: Cytochrome b-c1 complex subunit Rieske, mitochondrial
1D: Cytochrome b-c1 complex subunit Rieske, mitochondrial
1E: Cytochrome c1
1F: Cytochrome c1
1G: Complex III subunit 9
1H: Complex III subunit 9
1I: Cytochrome b-c1 complex subunit 6
1J: Cytochrome b-c1 complex subunit 6
1K: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8
1L: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8
1M: MPP-Beta
1N: MPP-Beta
1O: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10
1P: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10
1Q: Alpha-MPP
1R: Cytochrome b-c1 complex subunit 7
1S: Alpha-MPP
1T: Cytochrome b-c1 complex subunit 7
2A: Cytochrome c oxidase subunit 1
2B: Cytochrome c oxidase polypeptide II
2C: cytochrome-c oxidase
2D: Cytochrome c oxidase subunit 3
2E: Cox5b
2F: Cox5c
2G: Cox6a
2H: Cox6b
2I: Cox7c
2J: Cytochrome c oxidase subunit
2K: Cox7a
2L: CoxIn
3A: Cytochrome c oxidase subunit 1
3B: Cytochrome c oxidase polypeptide II
3C: cytochrome-c oxidase
3D: Cytochrome c oxidase subunit 3
3E: Cox5b
3F: Cox5c
3G: Cox6a
3H: Cox6b
3I: Cox7c
3J: Cytochrome c oxidase subunit
3K: Cox7a
3L: CoxIn
A: NADH:ubiquinone oxidoreductase 24 kD subunit
B: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
C: NADH:ubiquinone oxidoreductase 78 kDa subunit
D: NADH:ubiquinone oxidoreductase 30kDa subunit domain-containing protein
E: NADH:ubiquinone oxidoreductase 49 kD subunit
F: NADH:ubiquinone oxidoreductase subunit 10
G: NADH:ubiquinone oxidoreductase subunit 8
H: B14.5a
I: Mitochondrial NADH:ubiquinone oxidoreductase 18 kDa subunit
J: Acyl carrier protein
K: NADH:ubiquinone oxidoreductase B14 subunit
L: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
M: NADH:ubiquinone oxidoreductase 13 kD-like subunit
N: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
O: NADH:ubiquinone oxidoreductase B8 subunit
P: Putative NADH:ubiquinone oxidoreductase 39 kDa subunit
Q: NADH-ubiquinone oxidoreductase chain 1
R: NADH-ubiquinone oxidoreductase chain 2
S: NADH-ubiquinone oxidoreductase chain 3
T: NADH-ubiquinone oxidoreductase chain 4
U: NADH dehydrogenase subunit 4L
V: NADH-ubiquinone oxidoreductase chain 5
W: NADH-ubiquinone oxidoreductase chain 6
X: ASHI
Y: P9
Z: KFYI
a: AGGG
b: ESSS
c: B9
d: Mitochondrial NADH:ubiquinone oxidoreductase 10 kDa subunit
e: Mitochondrial NADH:ubiquinone oxidoreductase 23 kDa subunit
f: Mitochondrial NADH:ubiquinone oxidoreductase 7.5 kDa subunit
g: Mitochondrial putative NADH:ubiquinone oxidoreductase 6.5 kDa subunit
h: Mitochondrial NADH:ubiquinone oxidoreductase 13 kDa subunit
i: NADH:ubiquinone oxidoreductase 15 kDa subunit-like
j: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
k: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
l: NADH:ubiquinone oxidoreductase 20,9 kD-like subunit
m: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
n: Putative NADH:ubiquinone oxidoreductase 12.5 kDa subunit
o: Putative NADH:ubiquinone oxidoreductase 17.8 kDa subunit
p: Mitochondrial NADH:ubiquinone oxidoreductase 16 kDa subunit
q: Mitochondrial NADH:ubiquinone oxidoreductase 19 kDa subunit
r: Acyl carrier protein
s: Mitochondrial NADH:ubiquinone oxidoreductase 32 kDa subunit
t: CAG2 - CA-like
u: CAG1
v: P10
w: Mitochondrial NADH:ubiquinone oxidoreductase 9 kDa subunit
x: NUOP8
y: NUOP7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)2,217,846202
Polymers2,139,06695
Non-polymers78,780107
Water42,6422367
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 27 types, 41 molecules 1A1B1E1F1G1H1M1N1Q1S2C3C2E3E2F3F2G3G2H3H2I3I2K3K2L3LHJrU...

#1: Protein Cytochrome b / Complex III subunit 3 / Complex III subunit III / Cytochrome b-c1 complex subunit 3 / Ubiquinol- ...Complex III subunit 3 / Complex III subunit III / Cytochrome b-c1 complex subunit 3 / Ubiquinol-cytochrome-c reductase complex cytochrome b subunit


Mass: 42356.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P23662
#3: Protein Cytochrome c1


Mass: 33868.195 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q9FQ96, quinol-cytochrome-c reductase
#4: Protein Complex III subunit 9


Mass: 7040.211 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JC51
#7: Protein MPP-Beta


Mass: 55121.215 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J5P7
#9: Protein Alpha-MPP


Mass: 49640.430 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IKI9
#13: Protein cytochrome-c oxidase / Cytochrome c oxidase polypeptide II


Mass: 17270.035 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q9AU02, cytochrome-c oxidase
#15: Protein Cox5b


Mass: 19051.588 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8HRZ4
#16: Protein Cox5c


Mass: 10886.307 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J7H8
#17: Protein Cox6a


Mass: 13985.016 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3D591
#18: Protein Cox6b


Mass: 17277.316 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IN92
#19: Protein Cox7c


Mass: 11356.865 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IU42
#21: Protein Cox7a


Mass: 6532.420 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3D1M1
#22: Protein CoxIn


Mass: 9905.305 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JEU7
#30: Protein B14.5a


Mass: 13790.122 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JHV4
#32: Protein Acyl carrier protein


Mass: 13682.473 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6UKY4
#43: Protein NADH dehydrogenase subunit 4L


Mass: 24258.357 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q84K56
#46: Protein ASHI


Mass: 17110.604 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JCW1
#47: Protein P9


Mass: 6764.642 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DYZ8
#48: Protein KFYI


Mass: 13848.634 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J6N0
#49: Protein AGGG


Mass: 14270.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J815
#50: Protein ESSS


Mass: 19630.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J843
#51: Protein B9


Mass: 7334.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IVG9
#55: Protein Mitochondrial putative NADH:ubiquinone oxidoreductase 6.5 kDa subunit


Mass: 6497.381 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QIV8, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#67: Protein CAG2 - CA-like


Mass: 31209.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JFK6
#68: Protein CAG1


Mass: 24319.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JHY4
#71: Protein NUOP8


Mass: 17157.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IS53
#72: Protein NUOP7


Mass: 13655.893 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JA22

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Cytochrome b-c1 complex subunit ... , 3 types, 6 molecules 1C1D1I1J1R1T

#2: Protein Cytochrome b-c1 complex subunit Rieske, mitochondrial


Mass: 28545.494 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q8HEB4, quinol-cytochrome-c reductase
#5: Protein Cytochrome b-c1 complex subunit 6


Mass: 7991.032 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J8N9
#10: Protein Cytochrome b-c1 complex subunit 7


Mass: 14062.162 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8HX89

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Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit ... , 2 types, 4 molecules 1K1L1O1P

#6: Protein Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8


Mass: 8678.994 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J7I9, quinol-cytochrome-c reductase
#8: Protein Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10


Mass: 6476.588 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J4K5, quinol-cytochrome-c reductase

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Cytochrome c oxidase ... , 4 types, 8 molecules 2A3A2B3B2D3D2J3J

#11: Protein Cytochrome c oxidase subunit 1 / Cytochrome c oxidase polypeptide I


Mass: 55056.773 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P08681, cytochrome-c oxidase
#12: Protein Cytochrome c oxidase polypeptide II


Mass: 30716.742 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q9AU05
#14: Protein Cytochrome c oxidase subunit 3


Mass: 41453.922 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q9FV97
#20: Protein Cytochrome c oxidase subunit


Mass: 11694.374 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q8LK22

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NADH:ubiquinone oxidoreductase ... , 11 types, 11 molecules ACDEFGKMOil

#23: Protein NADH:ubiquinone oxidoreductase 24 kD subunit


Mass: 30643.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6V9B3, NADH:ubiquinone reductase (H+-translocating)
#25: Protein NADH:ubiquinone oxidoreductase 78 kDa subunit


Mass: 78432.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6UKY6, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#26: Protein NADH:ubiquinone oxidoreductase 30kDa subunit domain-containing protein


Mass: 32178.600 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IHL3
#27: Protein NADH:ubiquinone oxidoreductase 49 kD subunit


Mass: 52672.461 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6V9A8, NADH:ubiquinone reductase (H+-translocating)
#28: Protein NADH:ubiquinone oxidoreductase subunit 10


Mass: 18144.184 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6V9B0, NADH:ubiquinone reductase (H+-translocating)
#29: Protein NADH:ubiquinone oxidoreductase subunit 8


Mass: 26530.150 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6V9B1, NADH:ubiquinone reductase (H+-translocating)
#33: Protein NADH:ubiquinone oxidoreductase B14 subunit


Mass: 16135.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6UKY9, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#35: Protein NADH:ubiquinone oxidoreductase 13 kD-like subunit


Mass: 16306.489 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6UP30, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#37: Protein NADH:ubiquinone oxidoreductase B8 subunit


Mass: 11012.532 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6V9A9, NADH:ubiquinone reductase (H+-translocating)
#57: Protein NADH:ubiquinone oxidoreductase 15 kDa subunit-like


Mass: 9565.950 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6TH88, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#60: Protein NADH:ubiquinone oxidoreductase 20,9 kD-like subunit


Mass: 13461.300 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6UP28, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase

+
NADH dehydrogenase [ubiquinone] ... , 6 types, 6 molecules BLNjkm

#24: Protein NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial


Mass: 52303.109 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: A8ICJ1, NADH:ubiquinone reductase (H+-translocating)
#34: Protein NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial


Mass: 20648.477 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6UP29
#36: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12


Mass: 18034.045 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6UP31
#58: Protein NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7


Mass: 10295.870 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6UKY7
#59: Protein NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / Complex I-B22 / NADH-ubiquinone oxidoreductase B22 subunit


Mass: 13951.051 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6UKY8
#61: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13


Mass: 16400.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6UP32

+
Mitochondrial NADH:ubiquinone oxidoreductase ... , 9 types, 9 molecules Idefhpqsw

#31: Protein Mitochondrial NADH:ubiquinone oxidoreductase 18 kDa subunit


Mass: 17977.553 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6UKY3, NADH:ubiquinone reductase (H+-translocating)
#52: Protein Mitochondrial NADH:ubiquinone oxidoreductase 10 kDa subunit


Mass: 9994.435 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QAY2, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#53: Protein Mitochondrial NADH:ubiquinone oxidoreductase 23 kDa subunit


Mass: 23390.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QAY4, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#54: Protein Mitochondrial NADH:ubiquinone oxidoreductase 7.5 kDa subunit


Mass: 7651.823 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QIV4, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#56: Protein Mitochondrial NADH:ubiquinone oxidoreductase 13 kDa subunit


Mass: 16187.231 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QIV9, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#64: Protein Mitochondrial NADH:ubiquinone oxidoreductase 16 kDa subunit


Mass: 15291.994 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QAY0, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#65: Protein Mitochondrial NADH:ubiquinone oxidoreductase 19 kDa subunit


Mass: 22349.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QAY1, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#66: Protein Mitochondrial NADH:ubiquinone oxidoreductase 32 kDa subunit / Putative gamma carbonic anhydrase


Mass: 32729.148 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6S7R7, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase
#70: Protein Mitochondrial NADH:ubiquinone oxidoreductase 9 kDa subunit


Mass: 12159.065 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q6QAY5, NADH:ubiquinone reductase (H+-translocating), NADH dehydrogenase

+
Putative NADH:ubiquinone oxidoreductase ... , 3 types, 3 molecules Pno

#38: Protein Putative NADH:ubiquinone oxidoreductase 39 kDa subunit


Mass: 43709.176 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6V506
#62: Protein Putative NADH:ubiquinone oxidoreductase 12.5 kDa subunit


Mass: 12542.351 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6V504
#63: Protein Putative NADH:ubiquinone oxidoreductase 17.8 kDa subunit


Mass: 17907.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6V505

+
NADH-ubiquinone oxidoreductase chain ... , 6 types, 6 molecules QRSTVW

#39: Protein NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase subunit 1


Mass: 31606.412 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: P11658, NADH:ubiquinone reductase (H+-translocating)
#40: Protein NADH-ubiquinone oxidoreductase chain 2 / NADH dehydrogenase subunit 2


Mass: 42763.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: N-ter extension visible in structure,N-ter extension visible in structure
Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: P08740, NADH:ubiquinone reductase (H+-translocating)
#41: Protein NADH-ubiquinone oxidoreductase chain 3 / NADH dehydrogenase subunit 3


Mass: 30207.529 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6V502
#42: Protein NADH-ubiquinone oxidoreductase chain 4 / NADH dehydrogenase subunit 4


Mass: 48766.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: P20113, NADH:ubiquinone reductase (H+-translocating)
#44: Protein NADH-ubiquinone oxidoreductase chain 5 / NADH dehydrogenase subunit 5


Mass: 59087.402 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: P08739, NADH:ubiquinone reductase (H+-translocating)
#45: Protein NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase subunit 6


Mass: 17756.295 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: P10329, NADH:ubiquinone reductase (H+-translocating)

+
Protein/peptide , 1 types, 1 molecules v

#69: Protein/peptide P10


Mass: 5122.813 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: Frame shifted version of CHLRE_08g368050v5, not in UNIPROT
Source: (natural) Chlamydomonas reinhardtii (plant)

+
Non-polymers , 20 types, 2474 molecules

#73: Chemical
ChemComp-UQ5 / 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE


Mass: 522.758 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C34H50O4
#74: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#75: 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.: 16 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#76: Chemical
ChemComp-3PH / 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / PHOSPHATIDIC ACID


Mass: 704.998 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: C39H77O8P
#77: Chemical...
ChemComp-PTY / PHOSPHATIDYLETHANOLAMINE


Mass: 734.039 Da / Num. of mol.: 21 / Source method: obtained synthetically / Formula: C40H80NO8P / Comment: phospholipid*YM
#78: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#79: Chemical
ChemComp-PC7 / (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE / PHOSPHATIDYLCHOLINE / 1-PALMITOYL-2-STEAROYL-PC


Mass: 763.100 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C42H85NO8P / Comment: phospholipid*YM
#80: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#81: Chemical
ChemComp-PGT / (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / PHOSPHATIDYLGLYCEROL / 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-RAC-(1-GLYCEROL)](SODIUM SALT)


Mass: 751.023 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C40H79O10P / Comment: phospholipid*YM
#82: Chemical
ChemComp-HEA / HEME-A


Mass: 852.837 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C49H56FeN4O6
#83: Chemical ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu
#84: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#85: Chemical ChemComp-CUA / DINUCLEAR COPPER ION


Mass: 127.092 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cu2
#86: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2
#87: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE


Mass: 456.344 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H21N4O9P
#88: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Fe4S4
#89: Chemical ChemComp-8Q1 / S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate / S-dodecanoyl-4'-phosphopantetheine


Mass: 540.651 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C23H45N2O8PS
#90: Chemical ChemComp-NDP / NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE


Mass: 745.421 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H30N7O17P3
#91: Chemical ChemComp-COO / CROTONYL COENZYME A


Mass: 835.608 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C25H40N7O17P3S
#92: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2367 / Source method: isolated from a natural source / Formula: H2O

+
Details

Has ligand of interestN
Has protein modificationY

-
Experimental details

-
Experiment

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

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Sample preparation

ComponentName: Chlamydomonas reinhardtii respirasome / Type: COMPLEX / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Buffer solutionpH: 7.5
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k)

-
Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.20.1_4487:model refinement
5cryoSPARCCTF correction
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
12cryoSPARCclassification
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.82 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 83443 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.006139259
ELECTRON MICROSCOPYf_angle_d0.865188735
ELECTRON MICROSCOPYf_dihedral_angle_d10.39120602
ELECTRON MICROSCOPYf_chiral_restr0.05320306
ELECTRON MICROSCOPYf_plane_restr0.00723689

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