5XVD
[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in an air-oxidized condition
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| L | 0005886 | cellular_component | plasma membrane |
| L | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| L | 0016151 | molecular_function | nickel cation binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| L | 0046872 | molecular_function | metal ion binding |
| M | 0005886 | cellular_component | plasma membrane |
| M | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| M | 0016151 | molecular_function | nickel cation binding |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| M | 0046872 | molecular_function | metal ion binding |
| S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| S | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| S | 0051536 | molecular_function | iron-sulfur cluster binding |
| T | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| T | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| T | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG L 601 |
| Chain | Residue |
| L | GLU42 |
| L | ALA498 |
| L | HIS552 |
| L | HOH745 |
| L | HOH747 |
| L | HOH791 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue NFV L 602 |
| Chain | Residue |
| L | HIS68 |
| L | ALA477 |
| L | PRO478 |
| L | ARG479 |
| L | LEU482 |
| L | VAL500 |
| L | PRO501 |
| L | SER502 |
| L | CSO546 |
| L | CYS549 |
| L | CYS61 |
| L | CYS64 |
| L | THR67 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL L 603 |
| Chain | Residue |
| L | ARG74 |
| L | GLU77 |
| L | VAL84 |
| L | ASN294 |
| L | HIS318 |
| L | HOH754 |
| L | HOH784 |
| L | HOH831 |
| L | HOH933 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL L 604 |
| Chain | Residue |
| L | ALA176 |
| L | GLN178 |
| L | GLU271 |
| L | TRP272 |
| L | ARG275 |
| L | ARG538 |
| L | NA605 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA L 605 |
| Chain | Residue |
| L | GLN178 |
| L | TYR269 |
| L | PRO270 |
| L | GLU271 |
| L | GOL604 |
| L | HOH1089 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 S 401 |
| Chain | Residue |
| S | HIS192 |
| S | CYS195 |
| S | ARG198 |
| S | CYS220 |
| S | LEU221 |
| S | CYS226 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue F3S S 402 |
| Chain | Residue |
| L | GLN216 |
| S | CYS235 |
| S | PHE240 |
| S | CYS255 |
| S | TYR256 |
| S | GLY257 |
| S | CYS258 |
| S | ASN259 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 S 403 |
| Chain | Residue |
| S | CYS22 |
| S | CYS25 |
| S | ASP81 |
| S | SER119 |
| S | CYS120 |
| S | CYS154 |
| S | 8JU404 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue 8JU S 404 |
| Chain | Residue |
| S | CYS22 |
| S | THR23 |
| S | GLY24 |
| S | CYS25 |
| S | ASP81 |
| S | GLY82 |
| S | GLY118 |
| S | SER119 |
| S | CYS120 |
| S | GLY153 |
| S | CYS154 |
| S | PRO155 |
| S | SF4403 |
| S | HOH508 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL S 405 |
| Chain | Residue |
| L | PHE458 |
| L | LYS460 |
| S | GLU209 |
| S | PHE210 |
| S | HIS270 |
| S | HOH513 |
| S | HOH580 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG M 601 |
| Chain | Residue |
| M | GLU42 |
| M | ALA498 |
| M | HIS552 |
| M | HOH724 |
| M | HOH729 |
| M | HOH786 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue NFV M 602 |
| Chain | Residue |
| M | SER502 |
| M | CSO546 |
| M | CYS549 |
| M | CYS61 |
| M | CYS64 |
| M | THR67 |
| M | HIS68 |
| M | ALA477 |
| M | PRO478 |
| M | ARG479 |
| M | LEU482 |
| M | VAL500 |
| M | PRO501 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue NA M 603 |
| Chain | Residue |
| M | GLN178 |
| M | TYR269 |
| M | PRO270 |
| M | GLU271 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 T 401 |
| Chain | Residue |
| T | HIS192 |
| T | CYS195 |
| T | ARG197 |
| T | ARG198 |
| T | CYS220 |
| T | LEU221 |
| T | CYS226 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue F3S T 402 |
| Chain | Residue |
| M | LYS211 |
| M | GLN216 |
| T | CYS235 |
| T | PHE240 |
| T | CYS255 |
| T | TYR256 |
| T | GLY257 |
| T | CYS258 |
| T | ASN259 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 T 403 |
| Chain | Residue |
| T | CYS22 |
| T | CYS25 |
| T | ASP81 |
| T | SER119 |
| T | CYS120 |
| T | GLY153 |
| T | CYS154 |
| T | 8JU404 |
| site_id | AD8 |
| Number of Residues | 14 |
| Details | binding site for residue 8JU T 404 |
| Chain | Residue |
| T | CYS22 |
| T | THR23 |
| T | GLY24 |
| T | CYS25 |
| T | ASP81 |
| T | GLY82 |
| T | GLY118 |
| T | SER119 |
| T | CYS120 |
| T | GLY153 |
| T | CYS154 |
| T | PRO155 |
| T | SF4403 |
| T | HOH511 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL T 405 |
| Chain | Residue |
| M | PHE458 |
| T | GLU209 |
| T | PHE210 |
| T | HIS270 |
| T | HOH557 |
| site_id | AE1 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide PRO M 545 and CSO M 546 |
| Chain | Residue |
| M | ILE13 |
| M | GLU14 |
| M | CYS61 |
| M | SER502 |
| M | TYR518 |
| M | ILE540 |
| M | PHE543 |
| M | ASP544 |
| M | MET547 |
| M | SER548 |
| M | CYS549 |
| M | ALA550 |
| M | NFV602 |
| M | HOH751 |
| site_id | AE2 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide CSO M 546 and MET M 547 |
| Chain | Residue |
| M | GLU14 |
| M | LEU17 |
| M | CYS61 |
| M | SER502 |
| M | SER506 |
| M | ASP544 |
| M | PRO545 |
| M | SER548 |
| M | CYS549 |
| M | ALA550 |
| M | VAL551 |
| M | NFV602 |
| M | HOH794 |
Functional Information from PROSITE/UniProt
| site_id | PS00507 |
| Number of Residues | 26 |
| Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGMEeivknrdprdawmivQRiCGVC |
| Chain | Residue | Details |
| L | ARG39-CYS64 |
| site_id | PS00508 |
| Number of Residues | 10 |
| Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCMSCav.H |
| Chain | Residue | Details |
| L | PHE543-HIS552 |
