Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033727 | molecular_function | aldehyde dehydrogenase (FAD-independent) activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES A 908 |
| Chain | Residue |
| A | GLN99 |
| A | CYS100 |
| A | GLY101 |
| A | CYS103 |
| A | CYS137 |
| A | ARG138 |
| A | CYS139 |
| A | ILE368 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES A 909 |
| Chain | Residue |
| A | CYS40 |
| A | GLU41 |
| A | GLY43 |
| A | GLN44 |
| A | CYS45 |
| A | GLY46 |
| A | CYS48 |
| A | CYS60 |
| A | GLY39 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 3PL A 912 |
| Chain | Residue |
| A | ILE255 |
| A | THR256 |
| A | HIS752 |
| A | CYS753 |
| A | ALA780 |
| A | HOH2825 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT A 913 |
| Chain | Residue |
| A | ARG460 |
| A | SER461 |
| A | LEU498 |
| A | ALA531 |
| A | PHE532 |
| A | TYR535 |
| A | GLY536 |
| A | GLN539 |
| A | HOH2928 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCT A 914 |
| Chain | Residue |
| A | LYS884 |
| A | GLY888 |
| A | ARG890 |
| A | TYR892 |
| A | HOH2984 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 915 |
| Chain | Residue |
| A | HOH2277 |
| A | HOH2282 |
| A | HOH2435 |
| A | HOH3347 |
| A | HOH3348 |
| A | HOH3349 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 916 |
| Chain | Residue |
| A | HOH3282 |
| A | HOH3283 |
| A | HOH3350 |
| A | HOH3351 |
| A | HOH3352 |
| A | HOH3353 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 917 |
| Chain | Residue |
| A | ASP263 |
| A | GLU899 |
| A | GLU903 |
| A | HOH2710 |
| A | HOH3331 |
| A | HOH3337 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 918 |
| Chain | Residue |
| A | HOH2963 |
| A | HOH3354 |
| A | HOH3355 |
| A | HOH3356 |
| A | HOH3357 |
| A | HOH3358 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 919 |
| Chain | Residue |
| A | TYR892 |
| A | ARG893 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 920 |
| Chain | Residue |
| A | LYS248 |
| A | PRO898 |
| A | GLU899 |
| site_id | BC3 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE PCD A 921 |
| Chain | Residue |
| A | HOH3122 |
| A | HOH3162 |
| A | HOH3163 |
| A | HOH3359 |
| A | GLN99 |
| A | CYS139 |
| A | GLY419 |
| A | THR420 |
| A | PHE421 |
| A | GLY422 |
| A | ALA531 |
| A | PHE532 |
| A | ARG533 |
| A | TRP650 |
| A | HIS653 |
| A | GLY654 |
| A | GLN655 |
| A | GLY656 |
| A | GLY660 |
| A | SER695 |
| A | GLY696 |
| A | GLY697 |
| A | ARG699 |
| A | GLN700 |
| A | GLN701 |
| A | LEU795 |
| A | SER797 |
| A | CYS799 |
| A | ASN800 |
| A | THR804 |
| A | GLN807 |
| A | ALA864 |
| A | SER865 |
| A | GLY866 |
| A | VAL867 |
| A | GLY868 |
| A | GLU869 |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CEQGQCGAC |
| Chain | Residue | Details |
| A | CYS40-CYS48 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | CYS40 | |
| A | CYS45 | |
| A | CYS48 | |
| A | CYS60 | |
| A | CYS100 | |
| A | CYS103 | |
| A | CYS137 | |
| A | CYS139 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS653 | |
| A | GLU869 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 105 |
| Chain | Residue | Details |
| A | GLU869 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
