6F2B
Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO1 with Fe(II)/alpha-ketoglutarate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| C | 0055114 | biological_process | obsolete oxidation-reduction process |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| D | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 A 401 |
| Chain | Residue |
| A | HIS178 |
| A | GLU180 |
| A | HIS314 |
| A | AKG402 |
| A | HOH536 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue AKG A 402 |
| Chain | Residue |
| A | LEU193 |
| A | THR204 |
| A | HIS314 |
| A | ARG316 |
| A | ARG328 |
| A | ARG332 |
| A | FE2401 |
| A | HOH533 |
| A | MET156 |
| A | LEU175 |
| A | HIS178 |
| A | GLU180 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 401 |
| Chain | Residue |
| B | HIS178 |
| B | GLU180 |
| B | HIS314 |
| B | AKG402 |
| B | HOH654 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue AKG B 402 |
| Chain | Residue |
| B | LEU175 |
| B | GLU180 |
| B | VAL191 |
| B | LEU193 |
| B | THR204 |
| B | HIS314 |
| B | ARG316 |
| B | ARG328 |
| B | LEU330 |
| B | ARG332 |
| B | FE2401 |
| B | HOH543 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 C 401 |
| Chain | Residue |
| C | HIS178 |
| C | GLU180 |
| C | HIS314 |
| C | AKG402 |
| C | HOH600 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue AKG C 402 |
| Chain | Residue |
| C | MET156 |
| C | LEU175 |
| C | HIS178 |
| C | GLU180 |
| C | LEU193 |
| C | THR204 |
| C | HIS314 |
| C | ARG316 |
| C | ARG328 |
| C | ARG332 |
| C | FE2401 |
| C | HOH556 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 D 401 |
| Chain | Residue |
| D | HIS178 |
| D | GLU180 |
| D | HIS314 |
| D | AKG402 |
| D | HOH693 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue AKG D 402 |
| Chain | Residue |
| D | LEU175 |
| D | HIS178 |
| D | GLU180 |
| D | LEU193 |
| D | THR204 |
| D | HIS314 |
| D | ARG316 |
| D | ARG328 |
| D | LEU330 |
| D | ARG332 |
| D | FE2401 |
| D | HOH517 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Z4Z5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
