Research workbench
AlphaFold monomer V2.0 prediction for DNA-dependent metalloprotease WSS1 homolog (Q9P7B5)
Analyse AlphaFold monomer V2.0 prediction for DNA-dependent metalloprotease WSS1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9P7B5
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x94796168cFf9bD786025A738B85f21667861E30A
- Molecule
- DNA-dependent metalloprotease WSS1 homolog
- UniProt
- Q9P7B5
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 39% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-dependent metalloprotease WSS1 homolog | protein | 283 | 39% helix, 12% strand | Q9P7B5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.48 | 0.76 | 23 | empty |
| 2 | 89 | 0.36 | 0.75 | 22 | empty |
| 3 | 52 | 0.26 | 0.73 | 13 | empty |
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 Q9P7B5
- Elsewhere: UniProt Q9P7B5 · AlphaFold DB Q9P7B5
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