Research workbench
The influence of temperature on lysozyme crystals. structure and dynamics of protein and water
Analyse The influence of temperature on lysozyme crystals. structure and dynamics of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LSA
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hen egg white lysozyme
- EC
- 3.2.1.17
- UniProt
- P00698
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hen egg white lysozyme (EC 3.2.1.17) | protein | 129 | 42% 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 | 53 | 0.32 | 0.77 | 13 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1LSA · The influence of temperature on lysozyme crystals. structure and dynamics of protein and… · 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 1LSA · PDBe 1LSA · UniProt P00698
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