MolNFT v1 · #420308 · protein
AlphaFold monomer V2.0 prediction for something about silencing protein 5 (Q99314)
Q99314: “AlphaFold monomer V2.0 prediction for something about silencing protein 5 (Q99314)”. 2 pockets (best druggability 0.47). MolNFT v1 #420308 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q99314
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Something about silencing protein 5
- UniProt
- Q99314
- Pockets
- 2 · best druggability 0.47
Structure
1 distinct chain · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Something about silencing protein 5 | protein | 248 | 26% helix, 29% strand | Q99314 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.47 | 0.74 | 30 | empty |
| 2 | 71 | 0.36 | 0.76 | 17 | empty |
Compared structures
- 7F5M · Crystal structure of SAS5 yeats domain in complex with H3K27BZ peptide · an experimental structure of the same protein · chain A against A, TM-score 0.55
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 Q99314
- Elsewhere: UniProt Q99314 · AlphaFold DB Q99314
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