6F9P
Crystal structure of the Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5 with Re(II)
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 | 3 |
| Details | binding site for residue CL A 401 |
| Chain | Residue |
| A | ARG338 |
| A | RE402 |
| A | HOH555 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue RE A 402 |
| Chain | Residue |
| A | HIS176 |
| A | GLU178 |
| A | HIS312 |
| A | CL401 |
| A | HOH555 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | THR165 |
| A | GLY166 |
| A | SER167 |
| A | ARG338 |
| A | ARG145 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | PHE191 |
| A | TYR193 |
| A | SER202 |
| A | THR203 |
| A | HIS312 |
| A | GLY313 |
| A | ARG334 |
| A | HOH549 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 401 |
| Chain | Residue |
| B | ARG314 |
| B | RE402 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue RE B 402 |
| Chain | Residue |
| B | HIS176 |
| B | GLU178 |
| B | HIS312 |
| B | CL401 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 401 |
| Chain | Residue |
| C | RE402 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue RE C 402 |
| Chain | Residue |
| C | HIS176 |
| C | GLU178 |
| C | HIS312 |
| C | CL401 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 401 |
| Chain | Residue |
| D | RE402 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue RE D 402 |
| Chain | Residue |
| D | HIS176 |
| D | GLU178 |
| D | HIS312 |
| D | CL401 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL D 403 |
| Chain | Residue |
| D | ASP172 |
| D | PHE174 |
| D | VAL175 |
| D | TRP284 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 404 |
| Chain | Residue |
| D | ARG145 |
| D | GLY166 |
| 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 |
