2V0Y
Crystal structure of apo C298S tryptophanase 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 | TRYPTOPHANASE | polymer | 467 | 52372.7 | 1 | UniProt (P0A853) Pfam (PF01212) In PDB | ESCHERICHIA COLI | L-TRYPTOPHAN INDOLE-LYASE, TNASE |
| 2 | A | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 3 | A | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 4 | water | water | 18.0 | 520 | Chemie (HOH) |
Sequence modifications
A: 5 - 471 (UniProt: P0A853)
| PDB | External Database | Details |
|---|---|---|
| Ser 298 | Cys 298 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 52372.7 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 59.8 | |
| All* | Total formula weight | 52432.5 |
