Research workbench
AlphaFold monomer V2.0 prediction for S-crystallin SL18 (P27016)
Analyse AlphaFold monomer V2.0 prediction for S-crystallin SL18 (P27016) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27016
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- S-crystallin SL18
- UniProt
- P27016
- Pockets
- 5 · best druggability 0.63
Structure
1 distinct chain · 46% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-crystallin SL18 | protein | 308 | 46% helix, 7% strand | P27016 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.63 | 0.84 | 23 | empty |
| 2 | 96 | 0.45 | 0.79 | 24 | empty |
| 3 | 85 | 0.39 | 0.77 | 14 | empty |
| 4 | 76 | 0.33 | 0.75 | 16 | empty |
| 5 | 60 | 0.26 | 0.72 | 15 | 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 P27016
- Elsewhere: UniProt P27016 · AlphaFold DB P27016
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