MolNFT v1 · #295429 · protein
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A1D432)
A1D432: “AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A1D432)”. 8 pockets (best druggability 0.76). MolNFT v1 #295429 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A1D432
- Type
- protein
- Length
- 967 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Vacuolar membrane protease
- UniProt
- A1D432
- Pockets
- 8 · best druggability 0.76
Structure
1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 967 | 39% helix, 17% strand | A1D432 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.76 | 0.78 | 102 | empty |
| 2 | 313 | 0.66 | 0.80 | 28 | empty |
| 3 | 104 | 0.63 | 0.89 | 19 | empty |
| 4 | 91 | 0.44 | 0.80 | 23 | empty |
| 5 | 165 | 0.43 | 0.75 | 31 | 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 A1D432
- Elsewhere: UniProt A1D432 · AlphaFold DB A1D432
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