4U9H
Ultra High Resolution Structure Of The Ni-R 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 SF4 S 1001 |
Chain | Residue |
L | HIS235 |
S | THR113 |
S | CYS114 |
S | GLY149 |
S | CYS150 |
S | PRO151 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SF4 S 1002 |
Chain | Residue |
S | LEU194 |
S | CYS216 |
S | LEU217 |
S | CYS222 |
S | HIS188 |
S | CYS191 |
S | ARG193 |
site_id | AC3 |
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 | AC4 |
Number of Residues | 5 |
Details | binding site for residue MPD S 1004 |
Chain | Residue |
L | MPD606 |
L | HOH996 |
S | ASN134 |
S | ASN146 |
S | HOH1226 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MPD S 1005 |
Chain | Residue |
S | ALA211 |
S | ARG212 |
S | GLY214 |
S | ASP244 |
S | HOH1151 |
S | HOH1220 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue MPD S 1006 |
Chain | Residue |
S | TYR164 |
S | HOH1179 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue MPD S 1007 |
Chain | Residue |
L | ALA169 |
L | LYS173 |
L | LEU213 |
S | HOH1113 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue NWN L 601 |
Chain | Residue |
L | ALA477 |
L | PRO478 |
L | ARG479 |
L | LEU482 |
L | VAL500 |
L | PRO501 |
L | SER502 |
L | CYS546 |
L | CYS549 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue MG L 602 |
Chain | Residue |
L | LEU498 |
L | HIS552 |
L | HOH726 |
L | HOH731 |
L | HOH737 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MPD L 603 |
Chain | Residue |
L | LYS321 |
L | MET379 |
L | HOH908 |
S | LEU194 |
S | ASP198 |
S | HOH1390 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue MPD L 604 |
Chain | Residue |
L | PRO359 |
L | LYS360 |
L | TYR361 |
L | HOH955 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue MPD L 605 |
Chain | Residue |
L | GLY193 |
L | GLY194 |
L | VAL458 |
L | HOH833 |
L | HOH1009 |
L | HOH1068 |
L | HOH1171 |
L | HOH1199 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue MPD L 606 |
Chain | Residue |
L | ASP166 |
L | ALA169 |
L | HOH711 |
S | LYS143 |
S | MPD1004 |
S | HOH1159 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue MPD L 607 |
Chain | Residue |
L | TYR307 |
L | LEU309 |
L | LYS332 |
L | PHE474 |
L | HOH777 |
L | HOH861 |
L | HOH994 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue MPD L 608 |
Chain | Residue |
L | GLU489 |
L | GLY494 |
L | HOH1056 |
L | HOH1196 |
S | PHE197 |
S | PHE202 |
S | TYR218 |
S | HOH1413 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue MPD L 609 |
Chain | Residue |
L | HOH1065 |
L | HOH1167 |
L | GLU348 |
L | TRP463 |
L | MET465 |
L | HOH852 |
L | HOH912 |
L | HOH1025 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue MPD L 610 |
Chain | Residue |
S | GLU172 |
S | HOH1105 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue TRS L 611 |
Chain | Residue |
L | GLU336 |
L | ALA349 |
L | HOH710 |
L | HOH876 |
L | HOH947 |
L | HOH1138 |
S | PRO263 |
S | GLN266 |
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 | CYS546 | |
L | CYS549 | |
L | HIS552 | |
S | CYS222 | |
S | CYS231 |