Research workbench
Crystal structure of naproxen esterase (carboxylesterase np) from bacillus subtilis
Analyse Crystal structure of naproxen esterase (carboxylesterase np) from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CCW
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxyl esterase np
- EC
- 3.1.1.1
- UniProt
- Q59248
- Ligands
- VKC
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxyl esterase np (EC 3.1.1.1) | protein | 285 | 43% helix, 19% strand | Q59248 |
Ligands and binding sites
- VKC · (2-hydroxyethoxy)acetic acid · ligand · 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 | 574 | 0.74 | 0.81 | 60 | VKC |
Compared structures
- 4CCW · Crystal structure of naproxen esterase (carboxylesterase NP) from Bacillus subtilis · 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 Q59248
- Elsewhere: RCSB PDB 4CCW · PDBe 4CCW · UniProt Q59248
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.