Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q46YS9)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q46YS9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q46YS9
- Type
- protein
- Length
- 633 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x356701dD1dB7AA99E5e866B5DfA659D570042607
- Molecule
- Chaperone protein htpg
- UniProt
- Q46YS9
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 633 | 42% helix, 21% strand | Q46YS9 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 904 | 0.76 | 0.79 | 77 | empty |
| 2 | 105 | 0.68 | 0.91 | 22 | empty |
| 3 | 288 | 0.67 | 0.83 | 42 | empty |
| 4 | 142 | 0.50 | 0.79 | 27 | empty |
| 5 | 79 | 0.38 | 0.78 | 20 | 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 Q46YS9
- Elsewhere: UniProt Q46YS9 · AlphaFold DB Q46YS9
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