1ZIX
Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S, G211D, K234N)- 1.8 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 | 25505.6 | 1 | UniProt (P0A114) Pfam (PF01738) | Pseudomonas putida | Dienelactone hydrolase |
| 2 | B, C, D (A) | GLYCEROL | non-polymer | 92.1 | 3 | Chemie (GOL) | |||
| 3 | E (A) | water | water | 18.0 | 158 | Chemie (HOH) |
Sequence modifications
A: 1 - 236 (UniProt: P0A114)
| PDB | External Database | Details |
|---|---|---|
| Asp 36 | Glu 36 | engineered mutation |
| His 105 | Arg 105 | engineered mutation |
| Ser 123 | Cys 123 | engineered mutation |
| Asn 154 | Lys 154 | conflict |
| Asp 211 | Gly 211 | engineered mutation |
| Thr 224 | Arg 224 | conflict |
| Asn 234 | Lys 234 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 25505.6 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 276.3 | |
| All* | Total formula weight | 25781.9 |
