Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q3YSL9)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q3YSL9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3YSL9
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8320c2083B5a06fc519aB744C68C78731D2131C3
- Molecule
- Chaperone protein htpg
- UniProt
- Q3YSL9
- Pockets
- 7 · best druggability 0.78
Structure
1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 637 | 41% helix, 18% strand | Q3YSL9 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 267 | 0.78 | 0.90 | 41 | empty |
| 2 | 144 | 0.62 | 0.85 | 21 | empty |
| 3 | 333 | 0.55 | 0.75 | 31 | empty |
| 4 | 76 | 0.38 | 0.78 | 18 | empty |
| 5 | 69 | 0.35 | 0.76 | 11 | 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 Q3YSL9
- Elsewhere: UniProt Q3YSL9 · AlphaFold DB Q3YSL9
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