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1CZJ

CYTOCHROME C OF CLASS III (AMBLER) 26 KD

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 200
ChainResidue
APRO6
AGLU7
ASER8
AARG91
AARG95

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 119
ChainResidue
AHIS30
AHIS33
AILE36
ACYS38
ACYS41
AHIS42
AILE51
ASER53
ACYS54
AHEM121
ATHR2
APHE3
AVAL9
APHE28

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 120
ChainResidue
ACYS41
AHIS43
ATHR44
AGLU52
ASER53
ACYS54
ACYS59
AHIS60
AARG74
ATHR75
APHE76
ALYS84

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 121
ChainResidue
AVAL26
APHE28
AASN29
ASER32
AHIS33
AGLN40
AGLU83
ASER85
ACYS86
ACYS89
AHIS90
ALEU93
AASP100
APRO102
ACYS105
AASN106
AHEM119
AHOH201
AHOH227

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 122
ChainResidue
AMET11
APRO13
ATYR19
APRO21
ALYS22
ALYS23
AVAL26
AASN29
APHE76
AHIS77
ACYS86
AHIS90
ALEU103
AALA104
ACYS105
ACYS108
AHIS109
AHOH216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:8740362, ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ
ChainResidueDetails
AHIS30
AHIS33
AHIS42
AHIS43
AHIS60
AHIS77
AHIS90
AHIS109

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: covalent => ECO:0000269|PubMed:8740362, ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ
ChainResidueDetails
ACYS38
ACYS41
ACYS54
ACYS59
ACYS86
ACYS89
ACYS105
ACYS108

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PDB entries from 2024-11-13

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