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 |
| D | 0005737 | cellular_component | cytoplasm |
| 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 |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 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 | AKG302 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue AKG A 302 |
| Chain | Residue |
| A | THR138 |
| A | ALA272 |
| A | ARG281 |
| A | ARG285 |
| A | CO301 |
| A | ILE95 |
| A | ILE106 |
| A | GLY107 |
| A | HIS111 |
| A | ASP113 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CO G 301 |
| Chain | Residue |
| G | HIS111 |
| G | ASP113 |
| G | HIS270 |
| G | AKG302 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue AKG G 302 |
| Chain | Residue |
| G | ILE95 |
| G | HIS111 |
| G | ASP113 |
| G | THR138 |
| G | HIS270 |
| G | ALA272 |
| G | ARG281 |
| G | ARG285 |
| G | CO301 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue CFA G 303 |
| Chain | Residue |
| G | LEU83 |
| G | ARG104 |
| G | ILE106 |
| G | HIS111 |
| G | ASP113 |
| G | SER114 |
| G | VAL170 |
| G | PHE182 |
| G | VAL220 |
| G | TYR221 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CO D 301 |
| Chain | Residue |
| D | HIS111 |
| D | ASP113 |
| D | HIS270 |
| D | AKG302 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue AKG D 302 |
| Chain | Residue |
| D | ILE95 |
| D | HIS111 |
| D | ASP113 |
| D | THR138 |
| D | HIS270 |
| D | ALA272 |
| D | ARG281 |
| D | ARG285 |
| D | CO301 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue CFA D 303 |
| Chain | Residue |
| D | VAL80 |
| D | ILE82 |
| D | ILE106 |
| D | GLY107 |
| D | HIS111 |
| D | ASP113 |
| D | SER114 |
| D | TYR221 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CO J 301 |
| Chain | Residue |
| J | HIS111 |
| J | ASP113 |
| J | HIS270 |
| J | AKG302 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue AKG J 302 |
| Chain | Residue |
| J | GLY107 |
| J | HIS111 |
| J | ASP113 |
| J | THR138 |
| J | TRP263 |
| J | HIS270 |
| J | ALA272 |
| J | ARG281 |
| J | ARG285 |
| J | CO301 |
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"}]} |
