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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9W2Z

Cryo-EM structure of complex IV on the bovine heart submitochondrial particles, IV-A

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues56
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH
ChainResidueDetails
ATRP236-HIS291
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM
ChainResidueDetails
BVAL159-MET207
site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL
ChainResidueDetails
FVAL69-LEU91
site_idPS01329
Number of Residues18
DetailsCOX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN
ChainResidueDetails
GILE55-ASN72
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues30
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=III","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues47
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"2165784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues56
DetailsTransmembrane: {"description":"Helical; Name=V","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues65
DetailsTransmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues39
DetailsTransmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues56
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues57
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=X","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues31
DetailsTransmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23537388","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"PubMed","id":"10338009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues30
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues13
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues139
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues192
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13073","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P20674","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20385840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27605664","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8638158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues46
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues10
DetailsMotif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues11
DetailsMotif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56391","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues22
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"O00483","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues44
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"O00483","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q62425","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00483","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails
AMET65metal ligand
ATHR294metal ligand
AVAL295metal ligand, proton acceptor, proton donor
AVAL320proton acceptor, proton donor, proton relay
ATRP323proton acceptor, proton donor, proton relay
AASP442proton acceptor, proton donor, proton relay
APRO95proton acceptor, proton donor, proton relay
APRO130proton acceptor, proton donor, proton relay
AGLY160proton acceptor, proton donor, proton relay
AALA161proton acceptor, proton donor, proton relay
ATYR244covalently attached, electrostatic stabiliser, metal ligand, radical stabiliser
ALEU246proton acceptor, proton donor, proton relay
ALEU248covalently attached, hydrogen radical donor, proton acceptor, proton donor, proton relay, single electron acceptor
ATHR259proton acceptor, proton donor, proton relay

251422

PDB entries from 2026-04-01

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