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 | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| S | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE L 565 |
| Chain | Residue |
| L | CYS75 |
| L | CYS546 |
| L | NI566 |
| L | HOH616 |
| L | HOH622 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI L 566 |
| Chain | Residue |
| L | CYS543 |
| L | CYS546 |
| L | FE565 |
| L | CYS72 |
| L | CYS75 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG L 567 |
| Chain | Residue |
| L | GLU53 |
| L | GLU334 |
| L | GLN494 |
| L | LEU495 |
| L | HIS549 |
| L | HOH632 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 S 265 |
| Chain | Residue |
| S | HIS184 |
| S | CYS187 |
| S | ARG189 |
| S | LEU190 |
| S | PHE193 |
| S | CYS212 |
| S | LEU213 |
| S | CYS218 |
| S | PRO221 |
| S | VAL239 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S S 266 |
| Chain | Residue |
| L | LYS225 |
| L | GLN230 |
| S | THR223 |
| S | ASN225 |
| S | CYS227 |
| S | TRP237 |
| S | PRO238 |
| S | CYS245 |
| S | LEU246 |
| S | CYS248 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 S 267 |
| Chain | Residue |
| L | ARG70 |
| L | HIS228 |
| S | CYS17 |
| S | CYS20 |
| S | GLY112 |
| S | THR113 |
| S | CYS114 |
| S | GLY146 |
| S | CYS147 |
| S | PRO148 |
| site_id | ACT |
| Number of Residues | 2 |
| Details | THE ACTIVE SITE CONTAINS TWO METALS: NI AND FE. THE NI ION IS COORDINATED BY TWO TERMINAL CYSTEINES CYS L 72 ? AND CYS L 543 ? AND TWO BRIDGING CYSTEINES BETWEEN FE AND NI, CYS L 75 ? AND CYS L 546 ?. |
Functional Information from PROSITE/UniProt
| site_id | PS00507 |
| Number of Residues | 26 |
| Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRaCGVC |
| Chain | Residue | Details |
| L | ARG50-CYS75 | |
| 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 | PHE540-HIS549 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| L | CYS72 | |
| S | CYS245 | |
| S | CYS248 | |
| L | CYS75 | |
| L | CYS543 | |
| L | CYS546 | |
| S | HIS184 | |
| S | CYS187 | |
| S | CYS212 | |
| S | CYS218 | |
| S | CYS227 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| S | THR18 | |
| L | CYS543 | |
| L | GLU25 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cc1 |
| Chain | Residue | Details |
| L | CYS543 | |
