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1CYC

THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC A 104
ChainResidue
ALYS13
ATYR48
AASN52
ATRP59
ATHR78
ALYS79
AMET80
APHE82
AHOH105
ACYS14
ACYS17
AHIS18
ALEU32
ALEU35
AARG38
ATHR40
ATYR46

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC B 104
ChainResidue
BLYS13
BCYS14
BCYS17
BHIS18
BLEU32
BLEU35
BARG38
BTHR40
BTYR46
BTYR48
BASN52
BTRP59
BTHR78
BLYS79
BMET80
BPHE82

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072
ChainResidueDetails
AALA15
AHIS18
BALA15
BHIS18

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072
ChainResidueDetails
ATHR19
AILE81
BTHR19
BILE81

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylglycine => ECO:0000269|PubMed:5106585
ChainResidueDetails
AASP2
BASP2

236963

PDB entries from 2025-06-04

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