Research workbench
Crystal structure of (+)-pulegone reductase from Mentha piperita
Analyse Crystal structure of (+)-pulegone reductase from Mentha piperita in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EQL
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.72
- Source
- Mentha piperita
- Molecule
- (+)-pulegone reductase
- EC
- 1.3.1.81
- UniProt
- Q6WAU0
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · resolution 2.72 · 1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | (+)-pulegone reductase (EC 1.3.1.81) | protein | 338 | 30% helix, 28% strand | Q6WAU0 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.67 | 0.84 | 48 | empty |
| 2 | 122 | 0.44 | 0.77 | 23 | empty |
| 3 | 78 | 0.43 | 0.80 | 13 | empty |
| 4 | 100 | 0.36 | 0.74 | 21 | empty |
Compared structures
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 Q6WAU0
- Elsewhere: RCSB PDB 7EQL · PDBe 7EQL · UniProt Q6WAU0
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