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1H1O

Acidithiobacillus ferrooxidans cytochrome c4 structure supports a complex-induced tuning of electron transfer

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1186
ChainResidue
AALA98
AGLY99
AGLU102
AALA171
AASP175
AHOH2112
AHOH2112
AHOH2113

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1187
ChainResidue
ALYS40
AASN84
AHOH2114
AHOH2115
AHOH2115
AHIS39

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 1189
ChainResidue
AHIS152

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 1387
ChainResidue
APRO117
AALA118
AGLU121
BHIS239
BLYS240
BSER241
BASN284
BGLY331
BZN1388
BHOH2067

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1388
ChainResidue
AGLU121
BHIS239
BSO41387
BHOH2068

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 1389
ChainResidue
BHIS352
BHOH2069

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 1390
ChainResidue
BARG234
BHIS297

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 1184
ChainResidue
ATYR42
AGLN46
APRO117
ACYS119
ACYS122
AHIS123
APRO134
ALEU136
ATYR143
ALEU148
APHE151
AARG156
AASN158
AMET161
AILE164
AILE168
AVAL176
AHEM1185
AHOH2080
AHOH2093
AHOH2110
AHOH2111

site_idAC9
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 1185
ChainResidue
AASP15
ACYS16
ACYS19
AHIS20
AILE31
APRO33
ATYR42
ALEU47
ATYR50
AARG55
AASP57
AASN59
AGLY60
ATYR63
AMET64
AVAL67
ALEU79
ATYR143
AGLN147
ATYR150
AHEM1184
AHOH2020
AHOH2042
BILE262
BTYR263

site_idBC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 1385
ChainResidue
BHEM1386
BHOH2045
BHOH2064
BHOH2065
BTYR242
BGLN246
BILE316
BCYS319
BCYS322
BHIS323
BPRO332
BPHE333
BPRO334
BLEU336
BTYR343
BGLN347
BLEU348
BARG356
BASN358
BLEU360
BMET361
BILE364
BVAL376

site_idBC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 1386
ChainResidue
ATYR29
BASP215
BCYS216
BVAL218
BCYS219
BHIS220
BILE231
BPRO233
BLEU235
BTYR242
BLEU247
BTYR250
BARG255
BASP257
BASN259
BGLY260
BTYR263
BMET264
BLEU279
BTYR343
BGLN347
BHEM1385
BHOH2013
BHOH2066

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1384
ChainResidue
ACYS122
BGLY324
BSER325
BGLN328
BHOH2063

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433
ChainResidueDetails
ACYS119
ACYS122
BCYS216
BCYS219
BCYS319
BCYS322
ACYS16
ACYS19

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433
ChainResidueDetails
BHIS220
BHIS323
AHIS20
AHIS123

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PDB entries from 2024-05-15

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