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6N6P

Crystal structure of [FeFe]-hydrogenase in the presence of 7 mM Sodium dithionite

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 Residues16
Detailsbinding site for residue 402 A 601
ChainResidue
AALA230
APRO354
ACYS355
ALYS358
APHE417
AMET497
ACYS503
ASF4602
APRO231
ASER232
AILE268
AALA272
ACYS299
APRO324
AGLN325
AMET353

site_idAC2
Number of Residues10
Detailsbinding site for residue SF4 A 602
ChainResidue
ACYS300
APRO301
APRO354
ACYS355
ASER357
AALA498
ACYS499
ACYS503
AGLY506
A402601

site_idAC3
Number of Residues9
Detailsbinding site for residue SF4 A 603
ChainResidue
ALEU140
ACYS157
AMET166
ACYS190
ALEU191
ALEU192
ACYS193
AGLY194
ACYS196

site_idAC4
Number of Residues11
Detailsbinding site for residue SF4 A 604
ChainResidue
ACYS147
ALEU148
ALEU149
ACYS150
AGLY151
ACYS153
AILE177
ACYS200
AVAL202
AALA204
ALEU205

site_idAC5
Number of Residues11
Detailsbinding site for residue SF4 A 605
ChainResidue
AHIS94
AGLU95
APHE96
ALYS97
ACYS98
ACYS101
AARG104
ACYS107
ALYS146
AVAL202
AALA203

site_idAC6
Number of Residues9
Detailsbinding site for residue FES A 606
ChainResidue
AALA32
ALEU33
ACYS34
APHE35
ALYS45
ACYS46
AGLU47
ACYS49
ACYS62

site_idAC7
Number of Residues10
Detailsbinding site for residue GOL A 607
ChainResidue
ALYS223
ALYS333
ALYS345
AVAL347
APHE348
ALEU372
AARG373
AASP376
AHOH805
AHOH1051

site_idAC8
Number of Residues8
Detailsbinding site for residue GOL A 608
ChainResidue
AARG104
AGLU105
AASN106
ACYS107
ALEU110
ALYS111
AHOH817
AHOH983

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 Residues77
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues39
DetailsDomain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10529166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9836629","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10529166","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10529166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9836629","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10529166","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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