1LY8
The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | Peroxidase | polymer | 343 | 35477.4 | 2 | UniProt (P28314) Pfam (PF00141) Pfam (PF11895) In PDB | Coprinopsis cinerea | |
| 2 | A, B | 2-acetamido-2-deoxy-beta-D-glucopyranose | non-polymer | 221.2 | 2 | Chemie (NAG) | |||
| 3 | A, B | beta-D-mannopyranose | non-polymer | 180.2 | 2 | Chemie (BMA) | |||
| 4 | A, B | alpha-D-mannopyranose | non-polymer | 180.2 | 2 | Chemie (MAN) | |||
| 5 | A, B | CALCIUM ION | non-polymer | 40.1 | 4 | Chemie (CA) | |||
| 6 | A, B | PROTOPORPHYRIN IX CONTAINING FE | non-polymer | 616.5 | 2 | Chemie (HEM) | |||
| 7 | A, B | GLYCEROL | non-polymer | 92.1 | 12 | Chemie (GOL) | |||
| 8 | water | water | 18.0 | 637 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 343 (UniProt: P28314)
| PDB | External Database | Details |
|---|---|---|
| Ser 49 | Ile 69 | engineered mutation |
| Ala 53 | Val 73 | engineered mutation |
| Ala 121 | Thr 141 | engineered mutation |
| Phe 166 | Met 186 | engineered mutation |
| Gly 239 | Glu 259 | engineered mutation |
| Ile 242 | Met 262 | engineered mutation |
| Phe 272 | Tyr 292 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 70954.9 | |
| Non-Polymers* | Number of molecules | 24 |
| Total formula weight | 3661.5 | |
| All* | Total formula weight | 74616.3 |
