1TOG
Hydrocinnamic acid-bound structure of SRHEPT + A293D 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, B | Aspartate aminotransferase | polymer | 396 | 43869.3 | 2 | UniProt (P00509) Pfam (PF00155) In PDB | Escherichia coli | Transaminase A, ASPAT |
2 | A, B | HYDROCINNAMIC ACID | non-polymer | 150.2 | 2 | Chemie (HCI) | |||
3 | water | water | 18.0 | 137 | Chemie (HOH) |
Sequence modifications
A, B: 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 |
Asp 293 | Ala 281 | engineered mutation |
Ser 297 | Asn 285 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 87738.6 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 300.3 | |
All* | Total formula weight | 88038.9 |