MolNFT v1 · #295428 · protein
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (E9EYB5)
E9EYB5: “AlphaFold monomer V2.0 prediction for vacuolar membrane protease (E9EYB5)”. 9 pockets (best druggability 0.76). MolNFT v1 #295428 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- E9EYB5
- Type
- protein
- Length
- 1,032 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Vacuolar membrane protease
- UniProt
- E9EYB5
- Pockets
- 9 · best druggability 0.76
Structure
1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 1032 | 38% helix, 17% strand | E9EYB5 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 980 | 0.76 | 0.79 | 96 | empty |
| 2 | 239 | 0.64 | 0.82 | 26 | empty |
| 3 | 102 | 0.59 | 0.87 | 17 | empty |
| 4 | 203 | 0.58 | 0.80 | 29 | empty |
| 5 | 213 | 0.54 | 0.78 | 30 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 E9EYB5
- Elsewhere: UniProt E9EYB5 · AlphaFold DB E9EYB5
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