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3CF4

Structure of the CODH component of the M. barkeri ACDS complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004601molecular_functionperoxidase activity
A0005506molecular_functioniron ion binding
A0006084biological_processacetyl-CoA metabolic process
A0015948biological_processmethanogenesis
A0016151molecular_functionnickel cation binding
A0016491molecular_functionoxidoreductase activity
A0018492molecular_functioncarbon-monoxide dehydrogenase (acceptor) activity
A0019385biological_processmethanogenesis, from acetate
A0042542biological_processresponse to hydrogen peroxide
A0043885molecular_functioncarbon-monoxide dehydrogenase (ferredoxin) activity
A0046872molecular_functionmetal ion binding
A0050418molecular_functionhydroxylamine reductase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
G0015948biological_processmethanogenesis
G0019385biological_processmethanogenesis, from acetate
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SF4 A 809
ChainResidue
ACYS73
AGLN75
ACYS77
ACYS77

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 A 810
ChainResidue
ACYS84
AGLY92
ACYS94
AARG104
AALA184
ACYS76
ATYR78
ACYS79
ATYR81
AGLY82

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 808
ChainResidue
AHIS250
ACYS278
ACYS587
AWCC811
AHOH827

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE WCC A 811
ChainResidue
AHIS250
ACYS277
ACYS323
AGLY522
ACYS523
APRO524
ACYS552
ACYS587
APHE634
ASER635
ALYS637
AFE808
ACMO812
AHOH827

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CMO A 812
ChainResidue
AHIS117
ACYS587
ALYS637
AILE641
AWCC811
AHOH827

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 813
ChainResidue
ACYS427
APRO428
AILE433
ACYS455
AILE456
ACYS458
AARG459
ACYS461

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 814
ChainResidue
ACYS417
AALA418
AASP419
ACYS420
AGLY421
ACYS423
AMET437
ACYS465

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 815
ChainResidue
AARG91
AGLU331
ALYS334
AARG459

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 816
ChainResidue
ATHR406
AASP407
ALYS477

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 817
ChainResidue
AARG571

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 818
ChainResidue
AMET708
ALYS711
ATRP730
AHIS734
AHOH951

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 819
ChainResidue
AGLU430
AHOH1017
AHOH1117
GLYS117
GARG141

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 820
ChainResidue
AARG353

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 821
ChainResidue
APRO67
AILE69
ALYS99
AHOH1216
GALA127
GPHE131

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 822
ChainResidue
ALYS735
ATHR760
AHOH1047

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 823
ChainResidue
ALEU108
AARG109
ATHR112
AVAL182
AGLN636

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 824
ChainResidue
AASP290
AARG291
AARG292
AARG607
AGLN796
AHOH1027

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 825
ChainResidue
AHOH1159
AARG607
AARG623
AGLN796
APRO797
AHOH999

site_idCC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 826
ChainResidue
AMET259
ALEU283
ATYR286
AGLU288
APRO293
APRO294
ATYR295
AALA296
AHOH929
AHOH959

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY G 171
ChainResidue
ATHR669
AGLU744
AHOH1177
GTRP99

site_idCC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL G 172
ChainResidue
ALEU424
ALEU425
AHOH1017
GLYS118
GARG141
GGLY142
GASN153
GHOH216
GHOH247

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG G 173
ChainResidue
GLEU134
GTHR136
GASN146
GTHR148
GHOH259

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CaDCGaCLlACP
ChainResidueDetails
ACYS417-PRO428

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675
ChainResidueDetails
ACYS73
ACYS77
ACYS323
ACYS523
ACYS552
ACYS587

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4
ChainResidueDetails
ACYS76
ACYS458
ACYS461
ACYS465
ACYS79
ACYS84
ACYS94
ACYS417
ACYS420
ACYS423
ACYS427
ACYS455

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18621675
ChainResidueDetails
AHIS117
AHIS250
ACYS278

218853

PDB entries from 2024-04-24

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