1ZIC
Crystal Structure Analysis of the dienelactone hydrolase (C123S, R206A) mutant- 1.7 A
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Carboxymethylenebutenolidase | polymer | 236 | 25409.6 | 1 | UniProt (P0A114) Pfam (PF01738) | Pseudomonas putida | Dienelactone hydrolase |
| 2 | B (A) | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
| 3 | C, D (A) | GLYCEROL | non-polymer | 92.1 | 2 | Chemie (GOL) | |||
| 4 | E (A) | water | water | 18.0 | 184 | Chemie (HOH) |
Sequence modifications
A: 1 - 236 (UniProt: P0A114)
| PDB | External Database | Details |
|---|---|---|
| Ser 123 | Cys 123 | engineered mutation |
| Asn 154 | Lys 154 | conflict |
| Ala 206 | Arg 206 | engineered mutation |
| Thr 224 | Arg 224 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 25409.6 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 280.3 | |
| All* | Total formula weight | 25689.9 |
