Research workbench
AlphaFold monomer V2.0 prediction for serine protease 27 (Q6BEA2)
Analyse AlphaFold monomer V2.0 prediction for serine protease 27 (Q6BEA2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6BEA2
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Serine protease 27
- UniProt
- Q6BEA2
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 9% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease 27 | protein | 328 | 9% helix, 27% strand | Q6BEA2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.52 | 0.84 | 20 | empty |
| 2 | 132 | 0.49 | 0.79 | 24 | empty |
| 3 | 84 | 0.39 | 0.77 | 20 | empty |
Modifications
Observed in the structure: 5 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 Q6BEA2
- Elsewhere: UniProt Q6BEA2 · AlphaFold DB Q6BEA2
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