Research workbench
Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
Analyse Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LW9
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- K, CL
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 164 | 62% helix, 8% strand | P00720 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- HED · 2-hydroxyethyl disulfide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.50 | 0.76 | 28 | K |
Compared structures
- 1LW9 · Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects… · 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 P00720
- Elsewhere: RCSB PDB 1LW9 · PDBe 1LW9 · UniProt P00720
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