1OUB
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | LYSOZYME | polymer | 130 | 14692.6 | 1 | UniProt (P61626) Pfam (PF00062) | Homo sapiens (human) | |
| 2 | B (A) | SODIUM ION | non-polymer | 23.0 | 1 | Chemie (NA) | |||
| 3 | C (A) | water | water | 18.0 | 175 | Chemie (HOH) |
Sequence modifications
A: 1 - 130 (UniProt: P61626)
| PDB | External Database | Details |
|---|---|---|
| Ala 100 | Val 118 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 14692.6 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 23.0 | |
| All* | Total formula weight | 14715.6 |
