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4U9I

High Resolution Structure Of The Ni-R 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 SF4 S 2001
ChainResidue
LHIS235
STHR113
SCYS114
SGLY149
SCYS150
SPRO151

site_idAC2
Number of Residues7
Detailsbinding site for residue SF4 S 2002
ChainResidue
SLEU194
SCYS216
SLEU217
SCYS222
SHIS188
SCYS191
SARG193

site_idAC3
Number of Residues10
Detailsbinding site for residue F3S S 2003
ChainResidue
LLYS232
LGLN237
STHR227
SASN229
SCYS231
SPHE236
STRP241
SCYS249
SILE250
SCYS252

site_idAC4
Number of Residues3
Detailsbinding site for residue MPD S 2004
ChainResidue
LHOH1151
SASN134
SASN146

site_idAC5
Number of Residues3
Detailsbinding site for residue MPD S 2005
ChainResidue
LGLU489
SPRO225
SHOH2275

site_idAC6
Number of Residues6
Detailsbinding site for residue MPD S 2006
ChainResidue
SALA211
SARG212
SGLY214
SASP244
SHOH2209
SHOH2252

site_idAC7
Number of Residues3
Detailsbinding site for residue MPD S 2007
ChainResidue
LASN310
LLYS315
SHOH2134

site_idAC8
Number of Residues3
Detailsbinding site for residue MPD S 2008
ChainResidue
LALA169
LHOH825
SHOH2157

site_idAC9
Number of Residues3
Detailsbinding site for residue MPD S 2009
ChainResidue
SLEU165
SHOH2134
SHOH2190

site_idAD1
Number of Residues9
Detailsbinding site for residue NWN L 601
ChainResidue
LALA477
LPRO478
LARG479
LLEU482
LVAL500
LPRO501
LSER502
LCYS546
LCYS549

site_idAD2
Number of Residues5
Detailsbinding site for residue MG L 602
ChainResidue
LLEU498
LHIS552
LHOH732
LHOH735
LHOH743

site_idAD3
Number of Residues3
Detailsbinding site for residue MPD L 603
ChainResidue
LTYR199
LLEU200
LLYS360

site_idAD4
Number of Residues5
Detailsbinding site for residue MPD L 604
ChainResidue
LTYR395
LSER396
LPRO417
LPHE421
LHOH750

site_idAD5
Number of Residues4
Detailsbinding site for residue TRS L 605
ChainResidue
LTYR199
LTHR362
LHOH708
LHOH779

Functional Information from PROSITE/UniProt
site_idPS00507
Number of Residues26
DetailsNI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRtCGVC
ChainResidueDetails
LARG59-CYS84

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
LCYS84
LLEU498
LCYS546
LCYS549
LHIS552
SCYS222
SCYS231

224004

PDB entries from 2024-08-21

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