Research workbench
E3 alpha-esterase-7 carboxylesterase
Analyse E3 alpha-esterase-7 carboxylesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CH5
- Type
- protein
- Length
- 566 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxylic ester hydrolase
- EC
- 3.1.1.-
- UniProt
- Q25252
- Ligands
- DPF
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxylic ester hydrolase (EC 3.1.1.-) | protein | 566 | 38% helix, 16% strand | Q25252 |
Ligands and binding sites
- DPF · Diethyl hydrogen phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 712 | 0.72 | 0.78 | 55 | DPF |
| 2 | 326 | 0.67 | 0.82 | 42 | empty |
| 3 | 215 | 0.61 | 0.81 | 37 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5CH5 · E3 alpha-esterase-7 carboxylesterase · 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 Q25252
- Elsewhere: RCSB PDB 5CH5 · PDBe 5CH5 · UniProt Q25252
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