MolNFT v1 · #17488 · protein
T4 lysozyme cavity mutant L99A/M102Q bound with 2-allylphenol
1OV5: “T4 lysozyme cavity mutant L99A/M102Q bound with 2-allylphenol”. X-ray diffraction, 2 ligands (2LP, CL), 2 pockets (best druggability 0.72). MolNFT v1 #17488 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OV5
- Type
- protein
- Length
- 162 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
- 2LP, CL
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 162 | 65% helix, 9% strand | P00720 |
Ligands and binding sites
- 2LP · 2-allylphenol · ligand · chains A
- 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
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.72 | 0.98 | 15 | 2LP |
| 2 | 299 | 0.54 | 0.75 | 33 | empty |
Compared structures
- 1OV5 · T4 Lysozyme Cavity Mutant L99a/M102Q Bound With 2-Allylphenol · 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 1OV5 · PDBe 1OV5 · UniProt P00720
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