Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9F60

Structure of the Chlamydomonas reinhardtii respiratory complex IV from respiratory supercomplex

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
2A0004129molecular_functioncytochrome-c oxidase activity
2A0005739cellular_componentmitochondrion
2A0005743cellular_componentmitochondrial inner membrane
2A0006119biological_processoxidative phosphorylation
2A0016020cellular_componentmembrane
2A0046872molecular_functionmetal ion binding
2A1902600biological_processproton transmembrane transport
2B0005739cellular_componentmitochondrion
2B0016020cellular_componentmembrane
2B0016491molecular_functionoxidoreductase activity
2B0031966cellular_componentmitochondrial membrane
2B1902600biological_processproton transmembrane transport
2C0004129molecular_functioncytochrome-c oxidase activity
2C0016020cellular_componentmembrane
2C0016491molecular_functionoxidoreductase activity
2C0046872molecular_functionmetal ion binding
2C1902600biological_processproton transmembrane transport
2D0004129molecular_functioncytochrome-c oxidase activity
2D0005739cellular_componentmitochondrion
2D0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
2D0016020cellular_componentmembrane
2D0016491molecular_functionoxidoreductase activity
2D0045277cellular_componentrespiratory chain complex IV
2D1902600biological_processproton transmembrane transport
2E0005739cellular_componentmitochondrion
2E0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
2G0016020cellular_componentmembrane
2H0004129molecular_functioncytochrome-c oxidase activity
2H0005739cellular_componentmitochondrion
2H0016020cellular_componentmembrane
2H1902600biological_processproton transmembrane transport
2I0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpafgivsqvvsffsqkpvfgltgmicamgaisllgfivwa..HH
ChainResidueDetails
2ATRP231-HIS285

site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpalgvkmdavpgrlnqvwmsinregvfygq......CselCganHsfM
ChainResidueDetails
2CVAL83-MET131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00401","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P00401","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"UniProtKB","id":"P00401","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon