6EUO
Crystal structure of APO Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5
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 | MLT402 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue MLT A 402 |
| Chain | Residue |
| A | HIS312 |
| A | ARG334 |
| A | MET336 |
| A | ARG338 |
| A | FE401 |
| A | HOH513 |
| A | HOH554 |
| A | VAL154 |
| A | LEU173 |
| A | HIS176 |
| A | GLU178 |
| A | PHE191 |
| 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 | HOH536 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | GLU53 |
| A | GLN140 |
| A | LEU150 |
| A | ASP356 |
| A | TYR358 |
| A | HOH601 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | ARG145 |
| A | THR165 |
| A | GLY166 |
| A | SER167 |
| A | ARG338 |
| A | HOH576 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS176 |
| B | GLU178 |
| B | HIS312 |
| B | MLT402 |
| B | HOH522 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue MLT B 402 |
| Chain | Residue |
| B | GLN144 |
| B | ARG145 |
| B | GLY166 |
| B | SER167 |
| B | GLU178 |
| B | ARG338 |
| B | FE401 |
| B | HOH522 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | GLN33 |
| D | LEU44 |
| D | HIS64 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | ARG353 |
| B | THR354 |
| B | ASP355 |
| B | MET361 |
| B | HOH527 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS176 |
| C | GLU178 |
| C | HIS312 |
| C | MLT402 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue MLT C 402 |
| Chain | Residue |
| C | GLY166 |
| C | HIS176 |
| C | GLU178 |
| C | PHE191 |
| C | HIS312 |
| C | ARG314 |
| C | ARG334 |
| C | MET336 |
| C | ARG338 |
| C | FE401 |
| C | SO4406 |
| C | HOH549 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | ILE58 |
| C | GLN140 |
| C | ASP356 |
| C | TYR358 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | GLN102 |
| C | ASP103 |
| C | GLY106 |
| C | PRO107 |
| C | ARG195 |
| C | GLU332 |
| C | HOH523 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 405 |
| Chain | Residue |
| C | THR23 |
| C | THR289 |
| C | ILE291 |
| C | ASN292 |
| C | ASP294 |
| C | HOH535 |
| C | HOH541 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 C 406 |
| Chain | Residue |
| C | ARG145 |
| C | THR165 |
| C | GLY166 |
| C | SER167 |
| C | ARG338 |
| C | MLT402 |
| C | HOH521 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | HIS176 |
| D | GLU178 |
| D | HIS312 |
| D | MLT402 |
| site_id | AD8 |
| Number of Residues | 10 |
| Details | binding site for residue MLT D 402 |
| Chain | Residue |
| D | GLY166 |
| D | LEU173 |
| D | GLU178 |
| D | HIS312 |
| D | GLY313 |
| D | ARG334 |
| D | MET336 |
| D | ARG338 |
| D | FE401 |
| D | HOH534 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 403 |
| Chain | Residue |
| D | ARG145 |
| D | THR165 |
| D | GLY166 |
| D | SER167 |
| D | ARG338 |
| D | HOH542 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Z4Z5 |
| Chain | Residue | Details |
| A | HIS176 | |
| D | HIS176 | |
| D | GLU178 | |
| D | HIS312 | |
| A | GLU178 | |
| A | HIS312 | |
| B | HIS176 | |
| B | GLU178 | |
| B | HIS312 | |
| C | HIS176 | |
| C | GLU178 | |
| C | HIS312 |
