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1ETP

CRYSTAL STRUCTURE OF CYTOCHROME C4 FROM PSEUDOMONAS STUTZERI

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 199
ChainResidue
AVAL13
AARG61
AGLU65
AMET66
AMET69
AILE81
ATYR145
ALYS148
AGLN149
AHEM200
AHOH205
ACYS14
AHOH207
AHOH275
ACYS17
AHIS18
APRO30
ALEU32
ATYR39
AGLN43
AILE47

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 200
ChainResidue
ATYR39
ALYS42
AGLN43
AALA118
ACYS119
ACYS122
AHIS123
APHE135
APRO136
ALEU138
ATYR145
AARG158
AASN160
AILE166
AMET167
AILE186
AHEM199
AHOH206

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 199
ChainResidue
APHE135
BVAL13
BCYS14
BCYS17
BHIS18
BPHE29
BPRO30
BLEU32
BTYR39
BGLN43
BLEU44
BILE47
BARG61
BGLU65
BMET66
BLEU70
BILE81
BTYR145
BLYS148
BGLN149
BHEM200
BHOH219
BHOH300

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 200
ChainResidue
AALA16
BTYR39
BLYS42
BGLN43
BALA118
BCYS119
BCYS122
BHIS123
BPHE135
BPRO136
BLEU138
BTYR145
BARG158
BASN160
BILE166
BMET167
BVAL170
BHEM199
BHOH211
BHOH220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"description":"covalent"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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