Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (B0DC53)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (B0DC53) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0DC53
- Type
- protein
- Length
- 1,019 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Vacuolar membrane protease
- UniProt
- B0DC53
- Pockets
- 11 · best druggability 0.79
Structure
1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 1019 | 40% helix, 17% strand | B0DC53 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1108 | 0.79 | 0.80 | 99 | empty |
| 2 | 647 | 0.67 | 0.76 | 61 | empty |
| 3 | 59 | 0.67 | 0.95 | 18 | empty |
| 4 | 327 | 0.62 | 0.78 | 47 | empty |
| 5 | 229 | 0.59 | 0.80 | 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 B0DC53
- Elsewhere: UniProt B0DC53 · AlphaFold DB B0DC53
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