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1RCP

CYTOCHROME C'

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 130
ChainResidue
AARG10
AMET88
ACYS118
ACYS121
AHIS122
AARG126
AHOH173
AHOH179
AGLU11
APHE14
ALYS15
AMET21
ATHR68
AGLU69
APHE81
AGLY85

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 130
ChainResidue
BARG10
BGLU11
BPHE14
BLYS15
BMET21
BTHR68
BGLU69
BILE74
BPHE81
BGLY85
BMET88
BTHR117
BCYS118
BCYS121
BHIS122
BTYR125
BARG126
BHOH154
BHOH176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15299853, ECO:0000269|PubMed:8676382, ECO:0007744|PDB:1CPQ, ECO:0007744|PDB:1CPR, ECO:0007744|PDB:1RCP
ChainResidueDetails
ALEU47
AALA48
BLEU47
BALA48

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:15299853, ECO:0000269|PubMed:8676382, ECO:0007744|PDB:1CPQ, ECO:0007744|PDB:1CPR, ECO:0007744|PDB:1RCP
ChainResidueDetails
AALA97
AASN100
BALA97
BASN100

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:15299853, ECO:0000269|PubMed:8676382, ECO:0007744|PDB:1CPQ, ECO:0007744|PDB:1CPR, ECO:0007744|PDB:1RCP
ChainResidueDetails
AALA101
BALA101

218853

PDB entries from 2024-04-24

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