3AAT
ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA 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 | 43609.2 | 1 | UniProt (P00509) Pfam (PF00155) | Escherichia coli | |
| 2 | B (A) | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
| 3 | C (A) | PYRIDOXAL-5'-PHOSPHATE | non-polymer | 247.1 | 1 | Chemie (PLP) |
Sequence modifications
A: 5 - 409 (UniProt: P00509)
| PDB | External Database | Details |
|---|---|---|
| Phe 386 | Arg 374 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 43609.2 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 343.2 | |
| All* | Total formula weight | 43952.4 |
