6GAM
Structure of E14Q variant of E. coli hydrogenase-2 (as-isolated enzyme)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| L | 0005515 | molecular_function | protein binding |
| 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 | 0005515 | molecular_function | protein 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 | 9 |
| Details | binding site for residue SF4 S 401 |
| Chain | Residue |
| S | HIS192 |
| S | CYS195 |
| S | ARG197 |
| S | ARG198 |
| S | CYS220 |
| S | LEU221 |
| S | TYR222 |
| S | CYS226 |
| S | GLY228 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue F3S S 402 |
| Chain | Residue |
| L | LYS211 |
| L | GLN216 |
| S | CYS235 |
| S | PHE240 |
| S | CYS255 |
| S | TYR256 |
| S | GLY257 |
| S | CYS258 |
| S | ASN259 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 S 403 |
| Chain | Residue |
| L | ARG59 |
| S | CYS22 |
| S | CYS25 |
| S | GLY118 |
| S | SER119 |
| S | CYS120 |
| S | GLY153 |
| S | CYS154 |
| S | PRO155 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue FCO L 601 |
| Chain | Residue |
| L | CYS64 |
| L | THR67 |
| L | HIS68 |
| L | ALA477 |
| L | PRO478 |
| L | ARG479 |
| L | LEU482 |
| L | VAL500 |
| L | PRO501 |
| L | SER502 |
| L | CYS549 |
| L | NI602 |
| L | HOH1041 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NI L 602 |
| Chain | Residue |
| L | CYS61 |
| L | CYS64 |
| L | CYS546 |
| L | CYS549 |
| L | FCO601 |
| L | HOH1041 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG L 603 |
| Chain | Residue |
| L | GLU42 |
| L | ALA498 |
| L | HIS552 |
| L | HOH726 |
| L | HOH732 |
| L | HOH739 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 T 401 |
| Chain | Residue |
| T | HIS192 |
| T | CYS195 |
| T | ARG197 |
| T | ARG198 |
| T | CYS220 |
| T | LEU221 |
| T | TYR222 |
| T | CYS226 |
| site_id | AC8 |
| 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 | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 T 403 |
| Chain | Residue |
| M | ARG59 |
| T | CYS22 |
| T | CYS25 |
| T | GLY118 |
| T | SER119 |
| T | CYS120 |
| T | GLY153 |
| T | CYS154 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue FCO M 601 |
| Chain | Residue |
| M | CYS64 |
| M | THR67 |
| M | HIS68 |
| M | ALA477 |
| M | PRO478 |
| M | ARG479 |
| M | LEU482 |
| M | VAL500 |
| M | PRO501 |
| M | SER502 |
| M | CYS549 |
| M | NI602 |
| M | HOH973 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NI M 602 |
| Chain | Residue |
| M | CYS61 |
| M | CYS64 |
| M | CYS546 |
| M | CYS549 |
| M | FCO601 |
| M | HOH973 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG M 603 |
| Chain | Residue |
| M | HOH726 |
| M | HOH750 |
| M | HOH753 |
| M | GLU42 |
| M | ALA498 |
| M | HIS552 |
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. FDPCMACav.H |
| Chain | Residue | Details |
| L | PHE543-HIS552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| L | CYS61 | |
| S | CYS255 | |
| S | CYS258 | |
| T | CYS22 | |
| T | CYS25 | |
| T | CYS120 | |
| T | CYS154 | |
| T | HIS192 | |
| T | CYS195 | |
| T | CYS220 | |
| T | CYS226 | |
| L | CYS64 | |
| T | CYS235 | |
| T | CYS255 | |
| T | CYS258 | |
| L | CYS546 | |
| L | CYS549 | |
| M | CYS61 | |
| M | CYS64 | |
| M | CYS546 | |
| M | CYS549 | |
| S | CYS235 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by HybD |
| Chain | Residue | Details |
| L | HIS552 | |
| M | HIS552 |
