Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6N59

1.0 Angstrom crystal structure of [FeFe]-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 Residues17
Detailsbinding site for residue 402 A 601
ChainResidue
AALA230
APRO354
ACYS355
ALYS358
APHE417
AMET497
ACYS503
ASF4602
AHOH715
APRO231
ASER232
AILE268
AALA272
ACYS299
APRO324
AGLN325
AMET353

site_idAC2
Number of Residues9
Detailsbinding site for residue SF4 A 602
ChainResidue
ACYS300
APRO301
ACYS355
ASER357
AALA498
ACYS499
ACYS503
AGLY506
A402601

site_idAC3
Number of Residues9
Detailsbinding site for residue SF4 A 603
ChainResidue
ACYS157
ATHR163
AMET166
ACYS190
ALEU191
ALEU192
ACYS193
AGLY194
ACYS196

site_idAC4
Number of Residues10
Detailsbinding site for residue SF4 A 604
ChainResidue
ACYS147
ALEU148
ALEU149
ACYS150
AGLY151
ACYS153
ACYS200
AVAL202
AALA204
ALEU205

site_idAC5
Number of Residues10
Detailsbinding site for residue SF4 A 605
ChainResidue
AHIS94
AGLU95
ALYS97
ACYS98
ACYS101
AARG104
ACYS107
ALYS146
AVAL202
AALA203

site_idAC6
Number of Residues8
Detailsbinding site for residue FES A 606
ChainResidue
ALEU33
ACYS34
APHE35
ALYS45
ACYS46
AGLU47
ACYS49
ACYS62

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL A 607
ChainResidue
ALYS223
ALYS333
ALYS345
AVAL347
APHE348
AARG373
AASP376
AHOH760
AHOH1078

site_idAC8
Number of Residues9
Detailsbinding site for residue GOL A 608
ChainResidue
AARG104
AGLU105
AASN106
ACYS107
ALEU110
ALYS111
AASN437
AHOH759
AHOH872

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon