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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9W2U

Cryo-EM structure of complex I on the bovine heart submitochondrial particles, open

Functional Information from GO Data
ChainGOidnamespacecontents
a0005739cellular_componentmitochondrion
a0005743cellular_componentmitochondrial inner membrane
a0045271cellular_componentrespiratory chain complex I
A0005743cellular_componentmitochondrial inner membrane
A0006120biological_processmitochondrial electron transport, NADH to ubiquinone
A0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
A0030964cellular_componentNADH dehydrogenase complex
A1902600biological_processproton transmembrane transport
b0005739cellular_componentmitochondrion
b0005743cellular_componentmitochondrial inner membrane
b0045271cellular_componentrespiratory chain complex I
d0005737cellular_componentcytoplasm
d0005739cellular_componentmitochondrion
d0005743cellular_componentmitochondrial inner membrane
d0032981biological_processmitochondrial respiratory chain complex I assembly
d0045271cellular_componentrespiratory chain complex I
D0003954molecular_functionNADH dehydrogenase activity
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0006120biological_processmitochondrial electron transport, NADH to ubiquinone
D0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
D0019826molecular_functionoxygen sensor activity
D0022008biological_processneurogenesis
D0032981biological_processmitochondrial respiratory chain complex I assembly
D0042063biological_processgliogenesis
D0045271cellular_componentrespiratory chain complex I
D0061351biological_processneural precursor cell proliferation
D0071453biological_processcellular response to oxygen levels
D1902600biological_processproton transmembrane transport
e0005739cellular_componentmitochondrion
e0005743cellular_componentmitochondrial inner membrane
e0005758cellular_componentmitochondrial intermembrane space
e0032981biological_processmitochondrial respiratory chain complex I assembly
e0045271cellular_componentrespiratory chain complex I
f0005739cellular_componentmitochondrion
f0005743cellular_componentmitochondrial inner membrane
f0045271cellular_componentrespiratory chain complex I
F0005743cellular_componentmitochondrial inner membrane
F0006120biological_processmitochondrial electron transport, NADH to ubiquinone
F0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
F0045271cellular_componentrespiratory chain complex I
F1902600biological_processproton transmembrane transport
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0005758cellular_componentmitochondrial intermembrane space
G0006120biological_processmitochondrial electron transport, NADH to ubiquinone
G0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
G0009055molecular_functionelectron transfer activity
G0032981biological_processmitochondrial respiratory chain complex I assembly
G0045271cellular_componentrespiratory chain complex I
G0045333biological_processcellular respiration
G1902600biological_processproton transmembrane transport
H0003954molecular_functionNADH dehydrogenase activity
H0005743cellular_componentmitochondrial inner membrane
H0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
H0009060biological_processaerobic respiration
H0032981biological_processmitochondrial respiratory chain complex I assembly
H0045271cellular_componentrespiratory chain complex I
H1902600biological_processproton transmembrane transport
J0005739cellular_componentmitochondrion
J0005743cellular_componentmitochondrial inner membrane
J0006120biological_processmitochondrial electron transport, NADH to ubiquinone
J0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
J0032981biological_processmitochondrial respiratory chain complex I assembly
J0045271cellular_componentrespiratory chain complex I
J1902600biological_processproton transmembrane transport
K0005743cellular_componentmitochondrial inner membrane
K0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
K0030964cellular_componentNADH dehydrogenase complex
K0045271cellular_componentrespiratory chain complex I
K1902600biological_processproton transmembrane transport
L0005743cellular_componentmitochondrial inner membrane
L0006120biological_processmitochondrial electron transport, NADH to ubiquinone
L0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
L0015990biological_processelectron transport coupled proton transport
L0032981biological_processmitochondrial respiratory chain complex I assembly
L0045271cellular_componentrespiratory chain complex I
m0005739cellular_componentmitochondrion
m0005743cellular_componentmitochondrial inner membrane
m0045271cellular_componentrespiratory chain complex I
M0003954molecular_functionNADH dehydrogenase activity
M0005743cellular_componentmitochondrial inner membrane
M0006120biological_processmitochondrial electron transport, NADH to ubiquinone
M0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
M0009060biological_processaerobic respiration
M0015990biological_processelectron transport coupled proton transport
M0032981biological_processmitochondrial respiratory chain complex I assembly
M0045271cellular_componentrespiratory chain complex I
M0048039molecular_functionubiquinone binding
n0005739cellular_componentmitochondrion
n0005743cellular_componentmitochondrial inner membrane
n0045271cellular_componentrespiratory chain complex I
N0005743cellular_componentmitochondrial inner membrane
N0006120biological_processmitochondrial electron transport, NADH to ubiquinone
N0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
N0032981biological_processmitochondrial respiratory chain complex I assembly
N0045271cellular_componentrespiratory chain complex I
N1902600biological_processproton transmembrane transport
O0005737cellular_componentcytoplasm
O0005739cellular_componentmitochondrion
O0005759cellular_componentmitochondrial matrix
O0006120biological_processmitochondrial electron transport, NADH to ubiquinone
O0045271cellular_componentrespiratory chain complex I
p0005739cellular_componentmitochondrion
p0005743cellular_componentmitochondrial inner membrane
p0045271cellular_componentrespiratory chain complex I
P0003954molecular_functionNADH dehydrogenase activity
P0005739cellular_componentmitochondrion
P0005743cellular_componentmitochondrial inner membrane
P0005759cellular_componentmitochondrial matrix
P0006744biological_processubiquinone biosynthetic process
P0007623biological_processcircadian rhythm
P0031966cellular_componentmitochondrial membrane
P0044877molecular_functionprotein-containing complex binding
P0045271cellular_componentrespiratory chain complex I
q0005739cellular_componentmitochondrion
q0005743cellular_componentmitochondrial inner membrane
q0045271cellular_componentrespiratory chain complex I
t0005739cellular_componentmitochondrion
t0005743cellular_componentmitochondrial inner membrane
t0045271cellular_componentrespiratory chain complex I
u0005739cellular_componentmitochondrion
u0005743cellular_componentmitochondrial inner membrane
u0042775biological_processmitochondrial ATP synthesis coupled electron transport
u0045271cellular_componentrespiratory chain complex I
v0005739cellular_componentmitochondrion
v0005743cellular_componentmitochondrial inner membrane
v0006120biological_processmitochondrial electron transport, NADH to ubiquinone
v0016491molecular_functionoxidoreductase activity
v0042773biological_processATP synthesis coupled electron transport
v0045271cellular_componentrespiratory chain complex I
V0005739cellular_componentmitochondrion
V0005743cellular_componentmitochondrial inner membrane
V0022904biological_processrespiratory electron transport chain
V0045271cellular_componentrespiratory chain complex I
W0005739cellular_componentmitochondrion
W0005743cellular_componentmitochondrial inner membrane
W0032981biological_processmitochondrial respiratory chain complex I assembly
W0045271cellular_componentrespiratory chain complex I
X0005739cellular_componentmitochondrion
X0005743cellular_componentmitochondrial inner membrane
X0005758cellular_componentmitochondrial intermembrane space
X0045271cellular_componentrespiratory chain complex I
Z0005634cellular_componentnucleus
Z0005654cellular_componentnucleoplasm
Z0005737cellular_componentcytoplasm
Z0005739cellular_componentmitochondrion
Z0005743cellular_componentmitochondrial inner membrane
Z0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
Z0045271cellular_componentrespiratory chain complex I
Z0045892biological_processnegative regulation of DNA-templated transcription
Z1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM
ChainResidueDetails
TASP39-MET54
UASP39-MET54
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI
ChainResidueDetails
TASP64-ILE76
UASP64-ILE76
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
ChainResidueDetails
ICYS77-PRO88
ICYS116-PRO127
site_idPS00535
Number of Residues12
DetailsCOMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK
ChainResidueDetails
DLEU83-LYS94
site_idPS00542
Number of Residues22
DetailsCOMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL
ChainResidueDetails
CGLU131-LEU152
site_idPS00641
Number of Residues18
DetailsCOMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
ChainResidueDetails
GPRO38-CYS55
site_idPS00642
Number of Residues13
DetailsCOMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
ChainResidueDetails
GCYS105-GLN117
site_idPS00643
Number of Residues11
DetailsCOMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
ChainResidueDetails
GARG152-PHE162
site_idPS00644
Number of Residues16
DetailsCOMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
ChainResidueDetails
FGLY180-SER195
site_idPS00645
Number of Residues12
DetailsCOMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
ChainResidueDetails
FGLU357-GLY368
site_idPS00667
Number of Residues16
DetailsCOMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GLLQpIaDAIKLFiKE
ChainResidueDetails
HGLY44-GLU59
site_idPS00668
Number of Residues14
DetailsCOMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLTEGEseLVs.G
ChainResidueDetails
HPRO197-GLY210
site_idPS01099
Number of Residues19
DetailsCOMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
ChainResidueDetails
EASP134-PRO152
site_idPS01150
Number of Residues17
DetailsCOMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP
ChainResidueDetails
BGLY135-PRO151
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1401
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Hydroxyarginine","evidences":[{"source":"PubMed","id":"23836892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91WD5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine","evidences":[{"source":"PubMed","id":"23836892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues157
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27509854","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LDX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6J6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"P19404","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues57
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues78
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues39
DetailsDomain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues56
DetailsDomain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q56223","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VD9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99LC3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"UniProtKB","id":"Q99LC3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DC69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DC69","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20433953","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ75","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQ75","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues150
DetailsDomain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CR21","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1907568","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"1907966","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q16718","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPP6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q63362","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CPP6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues41
DetailsDomain: {"description":"CHCH 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues43
DetailsDomain: {"description":"CHCH 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues30
DetailsMotif: {"description":"Cx9C motif 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues30
DetailsMotif: {"description":"Cx9C motif 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues10
DetailsMotif: {"description":"Cx9C motif 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues10
DetailsMotif: {"description":"Cx9C motif 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues24
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"12381726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17060615","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7958365","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues86
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"1518044","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI51
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q3UIU2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI52
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQZ6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI53
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O95168","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI54
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y6M9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI55
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CR61","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI56
Number of Residues1
DetailsLipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"PubMed","id":"1518044","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI57
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O96000","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI58
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"9827566","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI59
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"1426273","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI60
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z1P6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI61
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

256448

PDB entries from 2026-07-15

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