1AOR
STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| A | 0033726 | molecular_function | aldehyde ferredoxin oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| B | 0033726 | molecular_function | aldehyde ferredoxin oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 606 |
| Chain | Residue |
| A | GLU332 |
| A | HIS383 |
| B | GLU332 |
| B | HIS383 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 607 |
| Chain | Residue |
| A | HOH5012 |
| A | HOH5013 |
| A | HIS181 |
| A | PTE609 |
| A | HOH5011 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 606 |
| Chain | Residue |
| B | HIS181 |
| B | PTE608 |
| B | HOH5024 |
| B | HOH5025 |
| B | HOH5026 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 608 |
| Chain | Residue |
| A | THR73 |
| A | ARG76 |
| A | ARG182 |
| A | CYS288 |
| A | CYS291 |
| A | CYS295 |
| A | CYS494 |
| A | PHE496 |
| A | PTE609 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE PTE A 609 |
| Chain | Residue |
| A | ARG76 |
| A | ALA92 |
| A | ASN93 |
| A | SER94 |
| A | GLY95 |
| A | ARG182 |
| A | ALA183 |
| A | GLY185 |
| A | ARG186 |
| A | GLU311 |
| A | GLU313 |
| A | ASP338 |
| A | LEU342 |
| A | ASP343 |
| A | THR344 |
| A | ARG444 |
| A | HIS448 |
| A | ILE449 |
| A | LYS450 |
| A | ASP489 |
| A | LEU493 |
| A | CYS494 |
| A | LEU495 |
| A | PHE496 |
| A | NA607 |
| A | SF4608 |
| A | HOH5012 |
| A | HOH5115 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 B 607 |
| Chain | Residue |
| B | ARG76 |
| B | CYS288 |
| B | CYS291 |
| B | CYS295 |
| B | CYS494 |
| B | PHE496 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE PTE B 608 |
| Chain | Residue |
| B | ARG76 |
| B | ALA92 |
| B | ASN93 |
| B | SER94 |
| B | GLY95 |
| B | ARG182 |
| B | ALA183 |
| B | ALA184 |
| B | GLY185 |
| B | ARG186 |
| B | GLU311 |
| B | GLU313 |
| B | ASP338 |
| B | LEU342 |
| B | ASP343 |
| B | THR344 |
| B | ARG444 |
| B | ILE449 |
| B | LYS450 |
| B | ASP489 |
| B | LEU493 |
| B | CYS494 |
| B | LEU495 |
| B | PHE496 |
| B | NA606 |
| B | HOH5026 |
| B | HOH5032 |
| site_id | PT1 |
| Number of Residues | 1 |
| Details | TUNGSTOPTERIN COFACTOR CONSISTING OF A SINGLE TUNGSTEN CENTER BOUND TO TWO MOLYBDOPTERIN LIGANDS (SUBUNIT A) |
| Chain | Residue |
| A | PTE609 |
| site_id | PT2 |
| Number of Residues | 1 |
| Details | TUNGSTOPTERIN COFACTOR CONSISTING OF A SINGLE TUNGSTEN CENTER BOUND TO TWO MOLYBDOPTERIN LIGANDS (SUBUNIT B). |
| Chain | Residue |
| B | PTE608 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS288 | |
| A | CYS291 | |
| A | CYS295 | |
| A | CYS494 | |
| B | CYS288 | |
| B | CYS291 | |
| B | CYS295 | |
| B | CYS494 |
