1TOJ
Hydrocinnamic acid-bound structure of SRHEPT 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 | Aspartate aminotransferase | polymer | 396 | 43825.3 | 1 | UniProt (P00509) Pfam (PF00155) In PDB | Escherichia coli | Transaminase A, ASPAT |
| 2 | A | HYDROCINNAMIC ACID | non-polymer | 150.2 | 1 | Chemie (HCI) | |||
| 3 | water | water | 18.0 | 148 | Chemie (HOH) |
Sequence modifications
A: 5 - 400 (UniProt: P00509)
| PDB | External Database | Details |
|---|---|---|
| Thr 12 | Ala 8 | engineered mutation |
| Thr 13 | Pro 9 | engineered mutation |
| Asp 34 | Asn 30 | engineered mutation |
| Ser 109 | Thr 104 | engineered mutation |
| Llp 258 | Lys 246 | modified residue |
| Ala 261 | Gly 249 | engineered mutation |
| Gly 285 | Ser 273 | engineered mutation |
| Ser 297 | Asn 285 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 43825.3 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 150.2 | |
| All* | Total formula weight | 43975.5 |
