Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CO A 301 |
| Chain | Residue |
| A | HIS111 |
| A | ASP113 |
| A | HIS270 |
| A | AKG303 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue FTJ A 302 |
| Chain | Residue |
| A | LYS169 |
| A | TRP180 |
| A | PHE182 |
| A | VAL220 |
| A | TYR221 |
| A | AKG303 |
| A | HOH456 |
| A | ARG104 |
| A | GLY107 |
| A | HIS111 |
| A | ASP113 |
| A | SER114 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue AKG A 303 |
| Chain | Residue |
| A | ILE95 |
| A | GLY107 |
| A | HIS111 |
| A | ASP113 |
| A | MET126 |
| A | THR138 |
| A | HIS270 |
| A | ALA272 |
| A | ARG281 |
| A | ARG285 |
| A | CO301 |
| A | FTJ302 |
| A | HOH461 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | ARG72 |
| A | PRO76 |
| A | VAL77 |
| B | ARG72 |
| B | PRO76 |
| B | VAL77 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CO B 301 |
| Chain | Residue |
| B | HIS111 |
| B | ASP113 |
| B | HIS270 |
| B | AKG303 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue FTJ B 302 |
| Chain | Residue |
| B | ARG104 |
| B | GLY107 |
| B | ASP108 |
| B | ASP109 |
| B | HIS111 |
| B | ASP113 |
| B | SER114 |
| B | LYS169 |
| B | TRP180 |
| B | PHE182 |
| B | VAL220 |
| B | TYR221 |
| B | HOH408 |
| B | HOH481 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue AKG B 303 |
| Chain | Residue |
| B | ILE95 |
| B | HIS111 |
| B | ASP113 |
| B | MET126 |
| B | THR138 |
| B | HIS270 |
| B | ALA272 |
| B | ARG281 |
| B | ARG285 |
| B | CO301 |
| B | HOH435 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CO F 301 |
| Chain | Residue |
| F | HIS111 |
| F | ASP113 |
| F | HIS270 |
| F | AKG303 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue FTJ F 302 |
| Chain | Residue |
| F | ILE82 |
| F | ARG104 |
| F | GLY107 |
| F | HIS111 |
| F | ASP113 |
| F | SER114 |
| F | LYS169 |
| F | TRP180 |
| F | PHE182 |
| F | VAL220 |
| F | TYR221 |
| F | AKG303 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue AKG F 303 |
| Chain | Residue |
| F | ILE95 |
| F | HIS111 |
| F | ASP113 |
| F | MET126 |
| F | THR138 |
| F | HIS270 |
| F | ALA272 |
| F | ARG281 |
| F | ARG285 |
| F | CO301 |
| F | FTJ302 |
| F | HOH420 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CL F 304 |
| Chain | Residue |
| F | ARG72 |
| F | PRO76 |
| F | VAL77 |
| J | ARG72 |
| J | PRO76 |
| J | VAL77 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CO J 301 |
| Chain | Residue |
| J | ASP113 |
| J | HIS270 |
| J | AKG303 |
| J | HIS111 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue FTJ J 302 |
| Chain | Residue |
| J | ARG104 |
| J | GLY107 |
| J | ASP108 |
| J | HIS111 |
| J | ASP113 |
| J | SER114 |
| J | LYS169 |
| J | TRP180 |
| J | PHE182 |
| J | VAL220 |
| J | TYR221 |
| J | HOH424 |
| J | HOH461 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for residue AKG J 303 |
| Chain | Residue |
| J | ILE95 |
| J | GLY107 |
| J | HIS111 |
| J | ASP113 |
| J | MET126 |
| J | THR138 |
| J | HIS270 |
| J | ALA272 |
| J | ARG281 |
| J | ARG285 |
| J | CO301 |
| J | HOH445 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P37610","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Site: {"description":"Contributes to enantiospecificity","evidences":[{"source":"PubMed","id":"16731970","evidenceCode":"ECO:0000303"}]} |
