Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q47GZ8)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q47GZ8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q47GZ8
- Type
- protein
- Length
- 636 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB5421b6788433D11c92ee25039BE5189Ef459De4
- Molecule
- Chaperone protein htpg
- UniProt
- Q47GZ8
- Pockets
- 11 · best druggability 0.82
Structure
1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 636 | 41% helix, 19% strand | Q47GZ8 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.82 | 0.94 | 43 | empty |
| 2 | 398 | 0.69 | 0.81 | 42 | empty |
| 3 | 95 | 0.52 | 0.83 | 22 | empty |
| 4 | 143 | 0.51 | 0.80 | 22 | empty |
| 5 | 68 | 0.41 | 0.81 | 14 | 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 Q47GZ8
- Elsewhere: UniProt Q47GZ8 · AlphaFold DB Q47GZ8
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