Research workbench
Similar hydrophobic replacements of leu 99 and phe 153 within the core of T4 lysozyme have different structural and thermodynamic consequences
Analyse Similar hydrophobic replacements of leu 99 and phe 153 within the core of T4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L89
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T4 lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- CL
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T4 lysozyme (EC 3.2.1.17) | protein | 162 | 64% helix, 9% strand | P00720 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
- BME · Beta-mercaptoethanol · additive · 2 copies · 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 | 241 | 0.53 | 0.76 | 30 | empty |
Compared structures
- 1L89 · Similar hydrophobic replacements of leu 99 and phe 153 within the core of T4 lysozyme… · 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 1L89 · PDBe 1L89 · UniProt P00720
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