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1WUH

Three-Dimensional Structure Of The Ni-A State Of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F

Functional Information from GO Data
ChainGOidnamespacecontents
L0008901molecular_functionferredoxin hydrogenase activity
L0016151molecular_functionnickel cation binding
L0016491molecular_functionoxidoreductase activity
L0042597cellular_componentperiplasmic space
L0046872molecular_functionmetal ion binding
L0047806molecular_functioncytochrome-c3 hydrogenase activity
S0008901molecular_functionferredoxin hydrogenase activity
S0009055molecular_functionelectron transfer activity
S0009061biological_processanaerobic respiration
S0009375cellular_componentferredoxin hydrogenase complex
S0016020cellular_componentmembrane
S0016491molecular_functionoxidoreductase activity
S0042597cellular_componentperiplasmic space
S0044569cellular_component[Ni-Fe] hydrogenase complex
S0046872molecular_functionmetal ion binding
S0047806molecular_functioncytochrome-c3 hydrogenase activity
S0051536molecular_functioniron-sulfur cluster binding
S0051538molecular_function3 iron, 4 sulfur cluster binding
S0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG L 1005
ChainResidue
LGLU62
LLEU498
LHIS552
LHOH5001
LHOH5002
LHOH5003

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 S 1001
ChainResidue
SCYS17
SCYS20
STHR113
SCYS114
SGLY149
SCYS150
SPRO151
LARG79
LHIS235
SGLU16

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 S 1002
ChainResidue
SHIS188
SCYS191
SARG193
SLEU194
SCYS216
SLEU217
SCYS222

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE F3S S 1003
ChainResidue
LGLN237
STHR227
SASN229
SCYS231
SPHE236
STRP241
SCYS249
SILE250
SCYS252

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NFC L 1004
ChainResidue
LCYS81
LVAL83
LCSO84
LHIS88
LALA477
LPRO478
LARG479
LLEU482
LVAL500
LPRO501
LSER502
LCSO546
LCYS549

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MPD S 2001
ChainResidue
LPHE320
LLYS321
LMET379
LGLU381
SLEU194
SPRO195
SHOH5600
SHOH5603
SHOH5604

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD S 2002
ChainResidue
SPHE117
SASN134
SASN146
SHOH5298
SHOH5660
SHOH5667
SHOH5706

Functional Information from PROSITE/UniProt
site_idPS00507
Number of Residues26
DetailsNI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRtCGVC
ChainResidueDetails
LARG59-CSO84

site_idPS00508
Number of Residues10
DetailsNI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCIACgv.H
ChainResidueDetails
LPHE543-HIS552

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10378274, ECO:0000269|PubMed:9438867, ECO:0007744|PDB:1H2A, ECO:0007744|PDB:1H2R
ChainResidueDetails
LGLU62
SCYS249
SCYS252
LCYS81
LCSO84
LLEU498
LCSO546
LCYS549
LHIS552
SCYS222
SCYS231

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cc1
ChainResidueDetails
STHR18
LGLU34

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PDB entries from 2024-05-01

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