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 | 3 |
Details | BINDING SITE FOR RESIDUE CL A 916 |
Chain | Residue |
A | ARG460 |
A | TYR535 |
A | GLN539 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 917 |
Chain | Residue |
A | ASP263 |
A | GLU899 |
A | GLU903 |
A | HOH4178 |
A | HOH4272 |
A | HOH4345 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 918 |
Chain | Residue |
A | TYR892 |
A | ARG893 |
A | HOH4194 |
A | HOH5012 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 919 |
Chain | Residue |
A | HOH4217 |
A | HOH4424 |
A | HOH4801 |
A | HOH4802 |
A | HOH4950 |
A | HOH5038 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 920 |
Chain | Residue |
A | LYS248 |
A | PRO898 |
A | GLU899 |
A | HOH4410 |
A | HOH4546 |
site_id | AC6 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE PCD A 921 |
Chain | Residue |
A | GLN99 |
A | CYS139 |
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 | SER698 |
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 |
A | IPA914 |
A | HOH4127 |
A | HOH4395 |
site_id | AC7 |
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 | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FES A 909 |
Chain | Residue |
A | GLY39 |
A | CYS40 |
A | GLU41 |
A | GLY43 |
A | GLN44 |
A | CYS45 |
A | GLY46 |
A | CYS48 |
A | ARG58 |
A | CYS60 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA A 914 |
Chain | Residue |
A | ALA531 |
A | TYR535 |
A | GLY697 |
A | PCD921 |
A | HOH4375 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPA A 915 |
Chain | Residue |
A | VAL5 |
A | GLU12 |
A | ASN14 |
A | PRO416 |
A | TRP683 |
A | HOH4047 |
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 | CSA1 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 8799115, 9242907 |
Chain | Residue | Details |
A | GLU869 | |
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 |