Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (A6VXW3)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (A6VXW3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6VXW3
- Type
- protein
- Length
- 642 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Chaperone protein htpg
- UniProt
- A6VXW3
- Pockets
- 8 · best druggability 0.78
Structure
1 distinct chain · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 642 | 43% helix, 19% strand | A6VXW3 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 888 | 0.78 | 0.81 | 78 | empty |
| 2 | 73 | 0.69 | 0.95 | 23 | empty |
| 3 | 271 | 0.63 | 0.81 | 27 | empty |
| 4 | 301 | 0.57 | 0.77 | 28 | empty |
| 5 | 115 | 0.35 | 0.73 | 18 | 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 A6VXW3
- Elsewhere: UniProt A6VXW3 · AlphaFold DB A6VXW3
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