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 | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 301 |
| Chain | Residue |
| A | HIS101 |
| A | ASP103 |
| A | HIS251 |
| A | AKG302 |
| A | HOH401 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKG A 302 |
| Chain | Residue |
| A | ASP103 |
| A | THR130 |
| A | HIS251 |
| A | ARG253 |
| A | ARG263 |
| A | LEU265 |
| A | ARG267 |
| A | FE2301 |
| A | HOH401 |
| A | LEU84 |
| A | VAL92 |
| A | LEU98 |
| A | HIS101 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 B 301 |
| Chain | Residue |
| B | HIS101 |
| B | ASP103 |
| B | HIS251 |
| B | AKG302 |
| B | HOH521 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AKG B 302 |
| Chain | Residue |
| B | LEU84 |
| B | LEU98 |
| B | HIS101 |
| B | ASP103 |
| B | THR130 |
| B | HIS251 |
| B | ARG253 |
| B | ARG263 |
| B | ARG267 |
| B | FE2301 |
| B | 2TQ304 |
| B | HOH521 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| A | ARG186 |
| B | ILE4 |
| B | VAL5 |
| B | PHE7 |
| B | ARG38 |
| B | HOH423 |
| B | HOH443 |
| B | HOH461 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2TQ B 304 |
| Chain | Residue |
| B | HIS101 |
| B | ALA102 |
| B | ASP103 |
| B | GLY104 |
| B | GLY105 |
| B | LEU106 |
| B | LEU107 |
| B | TYR164 |
| B | TYR165 |
| B | ARG267 |
| B | GLN269 |
| B | AKG302 |
| B | HOH401 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 C 301 |
| Chain | Residue |
| C | HIS101 |
| C | ASP103 |
| C | HIS251 |
| C | AKG302 |
| C | HOH538 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AKG C 302 |
| Chain | Residue |
| C | HIS101 |
| C | ASP103 |
| C | THR130 |
| C | HIS251 |
| C | ARG253 |
| C | ARG263 |
| C | ARG267 |
| C | FE2301 |
| C | HOH538 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2TQ C 303 |
| Chain | Residue |
| C | HIS101 |
| C | ALA102 |
| C | ASP103 |
| C | GLY104 |
| C | GLY105 |
| C | LEU106 |
| C | TYR164 |
| C | TYR191 |
| C | ARG267 |
| C | GLN269 |
| C | HOH401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12611886","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {} |
