6F2A
Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO1 with Fe(II)/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 | 5 |
| Details | binding site for residue FE2 A 401 |
| Chain | Residue |
| A | HIS178 |
| A | GLU180 |
| A | HIS314 |
| A | ARG332 |
| A | LYS402 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue LYS A 402 |
| Chain | Residue |
| A | HIS178 |
| A | GLU180 |
| A | ASP234 |
| A | SER236 |
| A | ASP268 |
| A | LEU271 |
| A | ARG332 |
| A | FE2401 |
| A | HOH501 |
| A | HOH551 |
| A | GLU147 |
| A | GLN166 |
| A | THR167 |
| A | SER168 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue LYS A 403 |
| Chain | Residue |
| A | GLU240 |
| A | GLY241 |
| C | VAL56 |
| C | THR57 |
| C | HIS59 |
| C | ARG129 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue ACY A 404 |
| Chain | Residue |
| A | ALA69 |
| A | GLN72 |
| A | ARG351 |
| A | HOH594 |
| B | GLU88 |
| B | TRP91 |
| B | HOH508 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ACY A 405 |
| Chain | Residue |
| A | GLU88 |
| A | TRP91 |
| B | HIS65 |
| B | ALA69 |
| B | GLN72 |
| B | HOH507 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | LEU186 |
| A | VAL336 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 B 401 |
| Chain | Residue |
| B | HIS178 |
| B | GLU180 |
| B | HIS314 |
| B | ARG332 |
| B | LYS402 |
| B | HOH601 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue LYS B 402 |
| Chain | Residue |
| B | GLN166 |
| B | THR167 |
| B | SER168 |
| B | HIS178 |
| B | GLU180 |
| B | ASP234 |
| B | SER236 |
| B | ASP268 |
| B | LEU271 |
| B | ARG332 |
| B | FE2401 |
| B | HOH504 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 C 401 |
| Chain | Residue |
| C | HIS178 |
| C | GLU180 |
| C | HIS314 |
| C | LYS402 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue LYS C 402 |
| Chain | Residue |
| C | GLU147 |
| C | GLN166 |
| C | THR167 |
| C | SER168 |
| C | HIS178 |
| C | GLU180 |
| C | ASP234 |
| C | SER236 |
| C | ASP268 |
| C | LEU271 |
| C | ARG332 |
| C | FE2401 |
| C | HOH502 |
| C | HOH513 |
| C | HOH547 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue ACY C 403 |
| Chain | Residue |
| C | ARG310 |
| C | HOH644 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue ACY C 404 |
| Chain | Residue |
| C | HIS65 |
| C | ALA69 |
| C | GLN72 |
| C | HOH534 |
| C | HOH604 |
| D | GLU88 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 D 401 |
| Chain | Residue |
| D | HIS178 |
| D | GLU180 |
| D | HIS314 |
| D | ARG332 |
| D | LYS402 |
| D | HOH575 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for residue LYS D 402 |
| Chain | Residue |
| D | LEU271 |
| D | ARG332 |
| D | FE2401 |
| D | HOH501 |
| D | GLN166 |
| D | THR167 |
| D | SER168 |
| D | HIS178 |
| D | GLU180 |
| D | ASP234 |
| D | SER236 |
| D | ASP268 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue ACY D 403 |
| Chain | Residue |
| C | GLU88 |
| C | TRP91 |
| D | HIS65 |
| D | ALA69 |
| D | GLN72 |
| D | HOH519 |
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 |
