MolNFT v1 · #30427 · protein
HYDROLASE
255L · Lysozyme: “HYDROLASE”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.51). MolNFT v1 #30427 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 255L
- 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
- CL
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 164 | 63% helix, 9% strand | P00720 |
Ligands and binding sites
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 | 229 | 0.51 | 0.76 | 27 | empty |
Compared structures
- 255L · HYDROLASE · 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 255L · PDBe 255L · UniProt P00720
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