1WUJ
Three-Dimensional Structure Of The Ni-B State Of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F
Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0008901 | molecular_function | ferredoxin hydrogenase activity |
L | 0016151 | molecular_function | nickel cation binding |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0042597 | cellular_component | periplasmic space |
L | 0046872 | molecular_function | metal ion binding |
L | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
S | 0009055 | molecular_function | electron transfer activity |
S | 0009061 | biological_process | anaerobic respiration |
S | 0009375 | cellular_component | ferredoxin hydrogenase complex |
S | 0016020 | cellular_component | membrane |
S | 0016491 | molecular_function | oxidoreductase activity |
S | 0042597 | cellular_component | periplasmic space |
S | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
S | 0046872 | molecular_function | metal ion binding |
S | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
S | 0051536 | molecular_function | iron-sulfur cluster binding |
S | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
S | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG L 1005 |
Chain | Residue |
L | GLU62 |
L | LEU498 |
L | HIS552 |
L | HOH5001 |
L | HOH5002 |
L | HOH5003 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 S 1001 |
Chain | Residue |
S | CYS17 |
S | CYS20 |
S | THR113 |
S | CYS114 |
S | GLY149 |
S | CYS150 |
S | PRO151 |
L | ARG79 |
L | HIS235 |
S | GLU16 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 S 1002 |
Chain | Residue |
S | HIS188 |
S | CYS191 |
S | ARG193 |
S | LEU194 |
S | CYS216 |
S | LEU217 |
S | CYS222 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S S 1003 |
Chain | Residue |
L | LYS232 |
L | GLN237 |
S | THR227 |
S | ASN229 |
S | CYS231 |
S | PHE236 |
S | TRP241 |
S | CYS249 |
S | ILE250 |
S | CYS252 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NFO L 1004 |
Chain | Residue |
L | CYS81 |
L | CYS84 |
L | HIS88 |
L | ALA477 |
L | PRO478 |
L | ARG479 |
L | LEU482 |
L | VAL500 |
L | PRO501 |
L | SER502 |
L | CSO546 |
L | CYS549 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRtCGVC |
Chain | Residue | Details |
L | ARG59-CYS84 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCIACgv.H |
Chain | Residue | Details |
L | PHE543-HIS552 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10378274, ECO:0000269|PubMed:9438867, ECO:0007744|PDB:1H2A, ECO:0007744|PDB:1H2R |
Chain | Residue | Details |
L | GLU62 | |
S | CYS249 | |
S | CYS252 | |
L | CYS81 | |
L | CYS84 | |
L | LEU498 | |
L | CSO546 | |
L | CYS549 | |
L | HIS552 | |
S | CYS222 | |
S | CYS231 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cc1 |
Chain | Residue | Details |
S | THR18 | |
L | GLU34 |