6F6J
Crystal structure of the Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO1 with Fe(II)/succinate/(3S)-3-hydroxy-L-lysine
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 | 6 |
| Details | binding site for residue FE A 401 |
| Chain | Residue |
| A | HIS178 |
| A | GLU180 |
| A | HIS314 |
| A | SIN402 |
| A | CUW403 |
| A | HOH655 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue SIN A 402 |
| Chain | Residue |
| A | LEU193 |
| A | THR204 |
| A | HIS314 |
| A | ARG316 |
| A | ARG328 |
| A | LEU330 |
| A | ARG332 |
| A | FE401 |
| A | CUW403 |
| A | HOH593 |
| A | HOH655 |
| A | HOH702 |
| A | MET156 |
| A | SER168 |
| A | LEU175 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue CUW A 403 |
| Chain | Residue |
| A | GLU147 |
| A | GLN166 |
| A | THR167 |
| A | SER168 |
| A | HIS178 |
| A | GLU180 |
| A | ASP268 |
| A | ARG332 |
| A | FE401 |
| A | SIN402 |
| A | HOH521 |
| A | HOH677 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue ACT A 404 |
| Chain | Residue |
| A | ILE142 |
| A | LEU186 |
| A | ARG187 |
| A | VAL336 |
| A | ASP338 |
| A | ARG341 |
| A | SER342 |
| A | HOH501 |
| A | HOH541 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS178 |
| B | GLU180 |
| B | HIS314 |
| B | SIN402 |
| B | CUW403 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue SIN B 402 |
| Chain | Residue |
| B | MET156 |
| B | LEU175 |
| B | GLU180 |
| B | LEU193 |
| B | THR204 |
| B | HIS314 |
| B | ARG328 |
| B | ARG332 |
| B | FE401 |
| B | HOH588 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue CUW B 403 |
| Chain | Residue |
| B | GLN166 |
| B | THR167 |
| B | SER168 |
| B | GLU180 |
| B | ASP234 |
| B | SER236 |
| B | ASP268 |
| B | LEU271 |
| B | ARG332 |
| B | FE401 |
| B | HOH511 |
| B | HOH536 |
| B | HOH562 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS178 |
| C | GLU180 |
| C | HIS314 |
| C | SIN402 |
| C | CUW403 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residue SIN C 402 |
| Chain | Residue |
| C | MET156 |
| C | SER168 |
| C | LEU175 |
| C | HIS178 |
| C | GLU180 |
| C | LEU193 |
| C | THR204 |
| C | HIS314 |
| C | GLY315 |
| C | ARG316 |
| C | ARG328 |
| C | ARG332 |
| C | FE401 |
| C | CUW403 |
| C | HOH628 |
| C | HOH709 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue CUW C 403 |
| Chain | Residue |
| C | ASP268 |
| C | ARG332 |
| C | FE401 |
| C | SIN402 |
| C | HOH512 |
| C | HOH517 |
| C | HOH558 |
| C | HOH593 |
| C | GLU147 |
| C | GLN166 |
| C | THR167 |
| C | SER168 |
| C | LEU175 |
| C | HIS178 |
| C | GLU180 |
| C | ASP234 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | HIS178 |
| D | GLU180 |
| D | HIS314 |
| D | SIN402 |
| D | CUW403 |
| D | HOH595 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue SIN D 402 |
| Chain | Residue |
| D | MET156 |
| D | SER168 |
| D | LEU175 |
| D | HIS178 |
| D | THR204 |
| D | HIS314 |
| D | ARG316 |
| D | ARG328 |
| D | LEU330 |
| D | FE401 |
| D | CUW403 |
| D | HOH595 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for residue CUW D 403 |
| Chain | Residue |
| D | GLN166 |
| D | THR167 |
| D | SER168 |
| D | LEU175 |
| D | HIS178 |
| D | GLU180 |
| D | ASP234 |
| D | SER236 |
| D | ASP268 |
| D | LEU271 |
| D | ARG332 |
| D | FE401 |
| D | SIN402 |
| D | HOH502 |
| D | HOH630 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue ACT D 404 |
| Chain | Residue |
| C | GLN87 |
| C | GLU88 |
| C | TRP91 |
| C | HOH595 |
| D | HIS65 |
| D | ALA69 |
| D | GLN72 |
| D | HOH546 |
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 |
