6EXH
Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5 with Fe(II)/succinate/(4R)-4-hydroxy-L-lysine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 4 |
| Details | binding site for residue FE A 401 |
| Chain | Residue |
| A | HIS176 |
| A | GLU178 |
| A | HIS312 |
| A | SIN403 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue LYO A 402 |
| Chain | Residue |
| A | ASP230 |
| A | ARG338 |
| A | SIN403 |
| A | HOH622 |
| A | HOH639 |
| A | TRP112 |
| A | ARG145 |
| A | GLY166 |
| A | SER167 |
| A | GLU178 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue SIN A 403 |
| Chain | Residue |
| A | LEU173 |
| A | HIS176 |
| A | GLU178 |
| A | PHE191 |
| A | TYR193 |
| A | HIS312 |
| A | ARG314 |
| A | ARG334 |
| A | MET336 |
| A | ARG338 |
| A | FE401 |
| A | LYO402 |
| A | HOH513 |
| A | HOH517 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | THR354 |
| A | ASP355 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS176 |
| B | GLU178 |
| B | HIS312 |
| B | SIN403 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue LYO B 402 |
| Chain | Residue |
| B | GLN144 |
| B | GLN164 |
| B | GLY166 |
| B | HIS176 |
| B | GLU178 |
| B | ASP260 |
| B | ARG338 |
| B | SIN403 |
| B | HOH529 |
| B | HOH537 |
| B | HOH543 |
| B | HOH562 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue SIN B 403 |
| Chain | Residue |
| B | VAL154 |
| B | GLY166 |
| B | LEU173 |
| B | HIS176 |
| B | GLU178 |
| B | HIS312 |
| B | ARG314 |
| B | ARG334 |
| B | MET336 |
| B | ARG338 |
| B | FE401 |
| B | LYO402 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS176 |
| C | GLU178 |
| C | HIS312 |
| C | HOH565 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue LYO C 402 |
| Chain | Residue |
| C | GLN144 |
| C | GLN164 |
| C | THR165 |
| C | GLY166 |
| C | HIS176 |
| C | GLU178 |
| C | ASN232 |
| C | GLU263 |
| C | ARG338 |
| C | HOH528 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | GLN102 |
| C | ASP103 |
| C | GLY106 |
| C | PRO107 |
| C | ARG195 |
| C | GLU332 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | HIS176 |
| D | GLU178 |
| D | HIS312 |
| D | SIN402 |
| D | HOH572 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue SIN D 402 |
| Chain | Residue |
| D | HIS176 |
| D | GLU178 |
| D | PHE191 |
| D | TYR193 |
| D | HIS312 |
| D | GLY313 |
| D | ARG334 |
| D | MET336 |
| D | ARG338 |
| D | FE401 |
| D | LYO404 |
| D | HOH572 |
| D | HOH590 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL D 403 |
| Chain | Residue |
| D | ALA48 |
| D | HIS64 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for residue LYO D 404 |
| Chain | Residue |
| D | GLN164 |
| D | THR165 |
| D | GLY166 |
| D | HIS176 |
| D | GLU178 |
| D | ASP230 |
| D | ASN232 |
| D | ASP260 |
| D | ARG338 |
| D | SIN402 |
| D | HOH530 |
| D | GLN144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Z4Z5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






