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Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume and conserved buried water molecules
Analyse Thermal stability determinants of chicken egg-white lysozyme core mutants… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LSM
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Gallus gallus
- Molecule
- Hen egg white lysozyme
- EC
- 3.2.1.17
- UniProt
- P00698
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · resolution 1.7 · 1 distinct chain · 40% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hen egg white lysozyme (EC 3.2.1.17) | protein | 129 | 40% helix, 11% strand | P00698 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.32 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1LSM · Thermal stability determinants of chicken egg-white lysozyme core mutants… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00698
- Elsewhere: RCSB PDB 1LSM · PDBe 1LSM · UniProt P00698
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