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1AQE

CRYSTAL STRUCTURE OF THE Y73E MUTANT OF 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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 200
ChainResidue
AARG95
AHOH236
APRO6
AGLU7
ASER8
ATHR79
AARG91

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 119
ChainResidue
APHE3
AILE5
AMET11
APHE28
AHIS30
AHIS33
AILE36
ACYS38
ACYS41
AHIS42
AILE51
ASER53
ACYS54
AHEM121
AHOH241
AHOH245
AHOH247

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 120
ChainResidue
ACYS41
AHIS42
AHIS43
ATHR44
ASER53
ACYS54
ACYS59
AHIS60
AARG74
ATHR75
ALYS84
AHOH272
AHOH286
AHOH297
AHOH298

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 121
ChainResidue
ALYS23
AVAL26
APHE28
AASN29
ASER32
AHIS33
AGLN40
AGLU83
ALYS84
ASER85
ACYS86
ACYS89
AHIS90
ALEU93
AHEM119
AHEM122
AHOH207
AHOH238
AHOH265
AHOH274

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 122
ChainResidue
AMET11
APRO13
ATYR19
APRO21
ALYS22
ALYS23
AVAL26
AGLU73
APHE76
AHIS77
ACYS86
AHIS90
ALEU103
AALA104
ACYS105
ACYS108
AHIS109
AHEM121
AHOH209

site_idHE1
Number of Residues1
DetailsBIS-HISTIDINYL LIGATED IRON IN A PROTOPORPHYRIN IX COVALENTLY ATTACHED BY TWO CYSTEINES.
ChainResidue
AHEM119

site_idHE2
Number of Residues1
DetailsBIS-HISTIDINYL LIGATED IRON IN A PROTOPORPHYRIN IX COVALENTLY ATTACHED BY TWO CYSTEINES.
ChainResidue
AHEM120

site_idHE3
Number of Residues1
DetailsBIS-HISTIDINYL LIGATED IRON IN A PROTOPORPHYRIN IX COVALENTLY ATTACHED BY TWO CYSTEINES.
ChainResidue
AHEM121

site_idHE4
Number of Residues1
DetailsBIS-HISTIDINYL LIGATED IRON IN A PROTOPORPHYRIN IX COVALENTLY ATTACHED BY TWO CYSTEINES.
ChainResidue
AHEM122

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 2024-11-06

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