2V0I
Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | BIFUNCTIONAL PROTEIN GLMU | polymer | 456 | 49346.1 | 1 | UniProt (P43889) Pfam (PF12804) Pfam (PF00132) In PDB | HAEMOPHILUS INFLUENZAE | GLMU FROM HAEMOPHILIS INFLUENZAE |
| 2 | A | URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE | non-polymer | 607.4 | 1 | Chemie (UD1) | |||
| 3 | A | TETRAETHYLENE GLYCOL | non-polymer | 194.2 | 2 | Chemie (PG4) | |||
| 4 | A | DI(HYDROXYETHYL)ETHER | non-polymer | 106.1 | 1 | Chemie (PEG) | |||
| 5 | A | SULFATE ION | non-polymer | 96.1 | 6 | Chemie (SO4) | |||
| 6 | water | water | 18.0 | 304 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 49346.1 | |
| Non-Polymers* | Number of molecules | 10 |
| Total formula weight | 1678.3 | |
| All* | Total formula weight | 51024.4 |
