1DYG
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | T4 LYSOZYME | polymer | 164 | 18692.4 | 1 | UniProt (P00720) Pfam (PF00959) In PDB | Enterobacteria phage T4 | |
| 2 | A | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 3 | A | BETA-MERCAPTOETHANOL | non-polymer | 78.1 | 2 | Chemie (BME) | |||
| 4 | water | water | 18.0 | 131 | Chemie (HOH) |
Sequence modifications
A: 1 - 164 (UniProt: P00720)
| PDB | External Database | Details |
|---|---|---|
| Glu 131 | Val 131 | CONFLICT |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 18692.4 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 227.2 | |
| All* | Total formula weight | 18919.6 |
