113L
STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN 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 (A) | T4 LYSOZYME | polymer | 164 | 18698.5 | 1 | UniProt (P00720) Pfam (PF00959) | Enterobacteria phage T4 | |
2 | B, C (A) | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
3 | D, E (A) | BETA-MERCAPTOETHANOL | non-polymer | 78.1 | 2 | Chemie (BME) | |||
4 | F (A) | water | water | 18.0 | 149 | Chemie (HOH) |
Sequence modifications
A: 1 - 164 (UniProt: P00720)
PDB | External Database | Details |
---|---|---|
Arg 44 | Ser 44 | conflict |
Thr 54 | Cys 54 | conflict |
Ala 97 | Cys 97 | conflict |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 18698.5 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 227.2 | |
All* | Total formula weight | 18925.7 |