6EUR
Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5 with Fe(II)/alpha-ketoglutarate
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 | AKG402 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue AKG A 402 |
| Chain | Residue |
| A | HIS312 |
| A | ARG314 |
| A | ARG334 |
| A | MET336 |
| A | ARG338 |
| A | FE401 |
| A | HOH543 |
| A | HOH555 |
| A | LEU173 |
| A | HIS176 |
| A | GLU178 |
| A | PHE191 |
| A | TYR193 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | ARG353 |
| A | THR354 |
| A | ASP355 |
| A | MET361 |
| A | HOH589 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | GLU53 |
| A | GLN140 |
| A | ASP356 |
| A | TYR358 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | GLU53 |
| A | GLY148 |
| A | GLY149 |
| A | HOH644 |
| D | LYS159 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | ALA245 |
| A | SER246 |
| A | TYR249 |
| A | ARG258 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS176 |
| B | GLU178 |
| B | HIS312 |
| B | AKG402 |
| B | HOH620 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue AKG B 402 |
| Chain | Residue |
| B | VAL154 |
| B | HIS176 |
| B | GLU178 |
| B | PHE191 |
| B | TYR193 |
| B | HIS312 |
| B | GLY313 |
| B | ARG334 |
| B | MET336 |
| B | ARG338 |
| B | FE401 |
| B | HOH590 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | GLN33 |
| D | LEU44 |
| D | LEU45 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS176 |
| C | GLU178 |
| C | HIS312 |
| C | AKG402 |
| C | HOH595 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue AKG C 402 |
| Chain | Residue |
| C | VAL154 |
| C | LEU173 |
| C | HIS176 |
| C | GLU178 |
| C | PHE191 |
| C | TYR193 |
| C | HIS312 |
| C | GLY313 |
| C | ARG314 |
| C | ARG334 |
| C | ARG338 |
| C | FE401 |
| C | HOH528 |
| C | HOH556 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | GLU53 |
| C | GLN140 |
| C | ASP356 |
| C | TYR358 |
| C | HOH535 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | GLN102 |
| C | ASP103 |
| C | GLY106 |
| C | PRO107 |
| C | ARG195 |
| C | GLU332 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 405 |
| Chain | Residue |
| C | THR352 |
| C | THR354 |
| C | MET361 |
| C | ILE368 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | HIS176 |
| D | GLU178 |
| D | HIS312 |
| D | AKG402 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for residue AKG D 402 |
| Chain | Residue |
| D | ARG314 |
| D | ARG334 |
| D | MET336 |
| D | ARG338 |
| D | FE401 |
| D | LEU173 |
| D | HIS176 |
| D | GLU178 |
| D | PHE191 |
| D | TYR193 |
| D | HIS312 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 403 |
| Chain | Residue |
| D | ASP172 |
| D | PHE174 |
| D | VAL175 |
| D | ILE291 |
| D | HOH550 |
| D | HOH561 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL D 404 |
| Chain | Residue |
| D | TRP112 |
| D | ARG145 |
| D | SER167 |
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 |






