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3C8Y

1.39 Angstrom crystal structure of Fe-only hydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0008901molecular_functionferredoxin hydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HCN A 575
ChainResidue
AALA230
APRO354
ACYS355
ALYS358
APHE417
AMET497
ACYS503
APRO231
ASER232
AILE268
AALA272
ACYS299
APRO324
AGLN325
AMET353

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 A 576
ChainResidue
ACYS300
APRO301
ACYS355
ACYS499
ACYS503
AGLY506

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 577
ChainResidue
ACYS157
ATHR163
AMET166
ACYS190
ALEU191
ALEU192
ACYS193
AGLY194
ACYS196

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 A 578
ChainResidue
ACYS147
ALEU148
ALEU149
ACYS150
AGLY151
ACYS153
ACYS200
APRO201
AALA204
ALEU205

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 579
ChainResidue
AHIS94
AGLU95
APHE96
ALYS97
ACYS98
ACYS101
ACYS107
ALYS146
AALA203

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES A 580
ChainResidue
ALEU33
ACYS34
APHE35
ACYS46
AGLU47
ACYS49
ACYS62

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 581
ChainResidue
ALYS223
ALYS333
ALYS345
APHE348
AARG373
AASP376
AHOH1087

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 582
ChainResidue
AARG104
AASN106
ACYS107
ALEU110
ALYS111
AASN437
AHOH795
AHOH1008

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 583
ChainResidue
ALYS223
APHE348
AHOH701
AHOH846
AHOH855

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. ClLCGrCVnACG
ChainResidueDetails
ACYS147-GLY158
ACYS190-PRO201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629
ChainResidueDetails
ACYS34
ACYS193
ACYS196
ACYS200
ACYS300
ACYS355
ACYS499
ACYS46
ACYS49
ACYS62
ACYS147
ACYS150
ACYS153
ACYS157
ACYS190

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01184, ECO:0000269|PubMed:10529166
ChainResidueDetails
AHIS94

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01184, ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629
ChainResidueDetails
ACYS98
ACYS101
ACYS107

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10529166
ChainResidueDetails
ACYS503

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfe
ChainResidueDetails
ALYS358
ACYS299

222415

PDB entries from 2024-07-10

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