4J5I
Crystal structure of an alpha-ketoglutarate-dependent taurine dioxygenase from Mycobacterium smegmatis
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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 401 |
| Chain | Residue |
| A | HIS95 |
| A | ASP97 |
| A | HIS248 |
| A | HOH532 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | ASP220 |
| A | ARG221 |
| A | ARG224 |
| B | HOH509 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 401 |
| Chain | Residue |
| B | ASP97 |
| B | HIS248 |
| B | ARG263 |
| B | HOH580 |
| B | HIS95 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 401 |
| Chain | Residue |
| C | HIS95 |
| C | ASP97 |
| C | HIS248 |
| C | ARG263 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D 401 |
| Chain | Residue |
| D | HIS95 |
| D | ASP97 |
| D | HIS248 |
| D | ARG263 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE E 401 |
| Chain | Residue |
| E | HIS95 |
| E | ASP97 |
| E | HIS248 |
| E | ARG263 |
| E | HOH564 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE F 401 |
| Chain | Residue |
| F | HIS95 |
| F | ASP97 |
| F | HIS248 |
| F | ARG263 |
| F | HOH561 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 402 |
| Chain | Residue |
| F | GLU62 |
| F | GLY65 |
| F | HOH538 |
| F | HOH539 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE G 401 |
| Chain | Residue |
| G | HIS95 |
| G | ASP97 |
| G | HIS248 |
| G | ARG263 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE H 401 |
| Chain | Residue |
| H | HIS95 |
| H | ASP97 |
| H | HIS248 |
| H | ARG263 |
| H | HOH553 |
| H | HOH554 |
