1ZI9
Crystal Structure Analysis of the dienelactone hydrolase (E36D, C123S) mutant- 1.5 A
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | Carboxymethylenebutenolidase | polymer | 236 | 25481.7 | 1 | UniProt (P0A114) Pfam (PF01738) In PDB | Pseudomonas putida | Dienelactone hydrolase |
2 | A | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
3 | A | GLYCEROL | non-polymer | 92.1 | 4 | Chemie (GOL) | |||
4 | water | water | 18.0 | 185 | Chemie (HOH) |
Sequence modifications
A: 1 - 236 (UniProt: P0A114)
PDB | External Database | Details |
---|---|---|
Asp 36 | Glu 36 | engineered mutation |
Ser 123 | Cys 123 | engineered mutation |
Asn 154 | Lys 154 | conflict |
Thr 224 | Arg 224 | conflict |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 25481.7 | |
Non-Polymers* | Number of molecules | 5 |
Total formula weight | 464.4 | |
All* | Total formula weight | 25946.2 |