Research workbench
The alpha-esterase-7 carboxylesterase, E3, from the blowfly lucilia cuprina
Analyse The alpha-esterase-7 carboxylesterase, E3, from the blowfly lucilia cuprina in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FNG
- Type
- protein
- Length
- 566 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 alpha-esterase-7 caboxylesterase
- UniProt
- Q25252
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 alpha-esterase-7 caboxylesterase | protein | 566 | 38% helix, 16% strand | Q25252 |
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 | 644 | 0.73 | 0.80 | 50 | empty |
| 2 | 270 | 0.65 | 0.82 | 39 | empty |
| 3 | 161 | 0.59 | 0.83 | 35 | empty |
Compared structures
- 4FNG · The alpha-esterase-7 carboxylesterase, E3, from the blowfly Lucilia cuprina · 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 4FNG · PDBe 4FNG · UniProt Q25252
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