5EUG
CRYSTALLOGRAPHIC AND ENZYMATIC STUDIES OF AN ACTIVE SITE VARIANT H187Q OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE: CRYSTAL STRUCTURES OF MUTANT H187Q AND ITS URACIL COMPLEX
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | PROTEIN (GLYCOSYLASE) | polymer | 229 | 25696.1 | 1 | UniProt (P12295) Pfam (PF03167) | Escherichia coli | UDG, UNG |
| 2 | B (A) | URACIL | non-polymer | 112.1 | 1 | Chemie (URA) | |||
| 3 | C (A) | water | water | 18.0 | 251 | Chemie (HOH) |
Sequence modifications
A: 1 - 229 (UniProt: P12295)
| PDB | External Database | Details |
|---|---|---|
| Gln 187 | His 187 | engineered mutation |
| His 213 | Arg 213 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 25696.1 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 112.1 | |
| All* | Total formula weight | 25808.2 |
