1AAM
THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI
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 | 43805.2 | 1 | UniProt (P00509) Pfam (PF00155) | Escherichia coli | AspAT,Transaminase A |
2 | B (A) | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) |
Sequence modifications
A: 13 - 408 (UniProt: P00509)
PDB | External Database | Details |
---|---|---|
Asp 292 | Arg 280 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 43805.2 | |
Non-Polymers* | Number of molecules | 1 |
Total formula weight | 96.1 | |
All* | Total formula weight | 43901.3 |