1ASB
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | ASPARTATE AMINOTRANSFERASE | polymer | 396 | 43575.2 | 1 | UniProt (P00509) Pfam (PF00155) | Escherichia coli | |
| 2 | B (A) | PYRIDOXAL-5'-PHOSPHATE | non-polymer | 247.1 | 1 | Chemie (PLP) | |||
| 3 | C (A) | MALEIC ACID | non-polymer | 116.1 | 1 | Chemie (MAE) | |||
| 4 | D (A) | water | water | 18.0 | 20 | Chemie (HOH) |
Sequence modifications
A: 13 - 408 (UniProt: P00509)
| PDB | External Database | Details |
|---|---|---|
| Ala 223 | Asp 211 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 43575.2 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 363.2 | |
| All* | Total formula weight | 43938.4 |
