6VW8
Formate Dehydrogenase FdsABG subcomplex FdsBG from C. necator
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0045271 | cellular_component | respiratory chain complex I |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0045271 | cellular_component | respiratory chain complex I |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 301 |
| Chain | Residue |
| A | CYS86 |
| A | ALA90 |
| A | CYS91 |
| A | CYS127 |
| A | LEU128 |
| A | GLN130 |
| A | CYS131 |
| B | SER188 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue K A 302 |
| Chain | Residue |
| A | HIS112 |
| A | GLU123 |
| A | HIS71 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue FMN B 601 |
| Chain | Residue |
| B | GLY154 |
| B | ARG155 |
| B | GLY156 |
| B | LYS165 |
| B | ASN182 |
| B | ASP184 |
| B | GLU185 |
| B | GLY186 |
| B | TYR270 |
| B | GLY273 |
| B | GLU274 |
| B | GLU275 |
| B | ILE308 |
| B | ASN309 |
| B | ASN310 |
| B | SER313 |
| B | ALA490 |
| B | MET491 |
| B | HOH743 |
| B | HOH764 |
| B | HOH781 |
| B | HOH795 |
| B | HOH806 |
| B | HOH895 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue SF4 B 602 |
| Chain | Residue |
| B | VAL289 |
| B | SER442 |
| B | CYS443 |
| B | GLY444 |
| B | LYS445 |
| B | CYS446 |
| B | CYS449 |
| B | SER487 |
| B | LEU488 |
| B | CYS489 |
| B | MET491 |
| B | GLY492 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | LEU120 |
| B | ARG124 |
| B | ARG253 |
| B | HOH731 |
| B | HOH830 |
| B | HOH867 |
| D | MET1 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| B | ARG11 |
| D | ASN35 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue FES C 301 |
| Chain | Residue |
| C | CYS86 |
| C | ALA88 |
| C | ALA90 |
| C | CYS91 |
| C | CYS127 |
| C | LEU128 |
| C | GLN130 |
| C | CYS131 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue K C 302 |
| Chain | Residue |
| C | HIS71 |
| C | HIS112 |
| C | GLU123 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | binding site for residue FMN D 600 |
| Chain | Residue |
| D | GLY154 |
| D | ARG155 |
| D | GLY156 |
| D | LYS165 |
| D | ASN182 |
| D | ASP184 |
| D | GLU185 |
| D | GLY186 |
| D | TYR270 |
| D | GLY273 |
| D | GLU274 |
| D | GLU275 |
| D | ILE308 |
| D | ASN309 |
| D | ASN310 |
| D | SER313 |
| D | ALA490 |
| D | MET491 |
| D | HOH721 |
| D | HOH759 |
| D | HOH762 |
| D | HOH768 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue SF4 D 601 |
| Chain | Residue |
| D | GLY492 |
| D | VAL289 |
| D | SER442 |
| D | CYS443 |
| D | GLY444 |
| D | LYS445 |
| D | CYS446 |
| D | CYS449 |
| D | SER487 |
| D | CYS489 |
| D | MET491 |
Functional Information from PROSITE/UniProt
| site_id | PS00644 |
| Number of Residues | 16 |
| Details | COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYVCGEETALLES |
| Chain | Residue | Details |
| B | GLY266-SER281 |
| site_id | PS00645 |
| Number of Residues | 12 |
| Details | COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGkCtPCRiG |
| Chain | Residue | Details |
| B | GLU441-GLY452 |
| site_id | PS01099 |
| Number of Residues | 19 |
| Details | COMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DgqVTlepvyCLGqCacGP |
| Chain | Residue | Details |
| A | ASP117-PRO135 |
