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2AIU

Crystal Structure of Mouse Testicular Cytochrome C at 1.6 Angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A0006915biological_processapoptotic process
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0022904biological_processrespiratory electron transport chain
A0042743biological_processhydrogen peroxide metabolic process
A0046872molecular_functionmetal ion binding
A2001244biological_processpositive regulation of intrinsic apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
ALYS14
ASER48
ALYS74
AHOH304
AHOH361
AHOH369
AHOH477
AHOH483

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
AASN55
AGLY57
AHOH339
AHOH360
AHOH416
AHOH446
AHOH466
AHOH472
AHOH506
ALYS54

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEC A 200
ChainResidue
ALYS14
ACYS15
AGLN17
ACYS18
AHIS19
ATHR29
APRO31
ATHR41
AGLY42
ATYR49
ATHR50
AASN53
ALYS56
ATRP60
ATYR68
ATHR79
ALYS80
AMET81
AILE82
APHE83
ALEU99
AHOH313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"240690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"240690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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