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2BQ4

Crystal structure of type I cytochrome c3 from Desulfovibrio africanus

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0009055molecular_functionelectron transfer activity
B0009061biological_processanaerobic respiration
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A1119
ChainResidue
AASP10
ALEU12
AGLU20
ATYR21
AHEC1118

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1120
ChainResidue
BHEC1119
BASP10
BLEU12
BGLU20
BTYR21

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEC A1115
ChainResidue
APRO1
AGLN2
AVAL3
APRO4
AHIS11
APHE25
AHIS27
AHIS30
AALA39
ACYS40
ACYS43
AHIS44
AGLY54
AHEC1117
AHOH2130

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEC A1116
ChainResidue
ACYS43
AHIS44
AHIS45
ALYS46
ACYS56
AGLU59
AGLY60
ACYS61
AHIS62
AALA81
ASER84
ASER86
AMET88
ASER89
AHOH2131
AHOH2132
AHOH2133
BLYS28

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEC A1117
ChainResidue
APHE25
AALA29
AHIS30
ASER32
ALEU33
ATHR35
ACYS43
APRO87
AMET88
ASER89
ACYS90
ACYS93
AHIS94
AMET97
ATHR103
ATHR104
AGLY105
APRO106
AHEC1115
AHOH2134

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC A1118
ChainResidue
AILE9
AASP10
AHIS11
ALEU12
ASER13
AASN14
ALEU19
AGLU20
ATYR21
AVAL23
APHE68
AALA70
AMET79
APHE82
AHIS83
ACYS90
AGLN91
AHIS94
APRO106
ATHR107
ACYS109
ACYS112
AHIS113
ACA1119

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEC B1116
ChainResidue
BHEC1118
BHOH2010
BHOH2081
BHOH2141
BHOH2142
BHOH2143
BHOH2144
BHOH2145
BGLN2
BHIS11
BPHE25
BHIS27
BHIS30
BALA39
BCYS40
BCYS43
BHIS44
BILE53
BGLY54
BGLY55

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEC B1117
ChainResidue
ALYS28
BCYS43
BHIS45
BLYS46
BGLY55
BCYS56
BGLU59
BGLY60
BCYS61
BHIS62
BPRO75
BALA81
BSER84
BSER86
BMET88
BSER89
BHOH2146
BHOH2147

site_idAC9
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC B1118
ChainResidue
BPHE25
BALA29
BHIS30
BSER32
BLEU33
BTHR35
BCYS43
BPRO87
BSER89
BCYS90
BCYS93
BHIS94
BMET97
BTHR103
BTHR104
BGLY105
BPRO106
BGLN115
BHEC1116
BHOH2148
BHOH2149

site_idBC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC B1119
ChainResidue
BILE9
BASP10
BHIS11
BLEU12
BSER13
BASN14
BLEU19
BGLU20
BTYR21
BVAL23
BPHE68
BALA70
BMET79
BPHE82
BHIS83
BCYS90
BGLN91
BHIS94
BPRO106
BTHR107
BCYS109
BCYS112
BHIS113
BCA1120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16226767, ECO:0007744|PDB:2BQ4
ChainResidueDetails
AASP10
ALEU12
AGLU20
ATYR21
BASP10
BLEU12
BGLU20
BTYR21

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:16226767, ECO:0007744|PDB:2BQ4
ChainResidueDetails
AHIS27
BHIS30
BHIS44
BHIS45
BHIS62
BHIS83
BHIS94
BHIS113
AHIS30
AHIS44
AHIS45
AHIS62
AHIS83
AHIS94
AHIS113
BHIS27

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: covalent => ECO:0000269|PubMed:16226767, ECO:0007744|PDB:2BQ4
ChainResidueDetails
ACYS40
BCYS43
BCYS56
BCYS61
BCYS90
BCYS93
BCYS109
BCYS112
ACYS43
ACYS56
ACYS61
ACYS90
ACYS93
ACYS109
ACYS112
BCYS40

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PDB entries from 2024-11-13

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