130L
STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT
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 | 18614.3 | 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 | 165 | Chemie (HOH) |
Sequence modifications
A: 1 - 164 (UniProt: P00720)
PDB | External Database | Details |
---|---|---|
Thr 54 | Cys 54 | conflict |
Ala 97 | Cys 97 | conflict |
Ser 151 | Thr 151 | conflict |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 18614.3 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 227.2 | |
All* | Total formula weight | 18841.5 |