Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q2GFY5)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q2GFY5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2GFY5
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Chaperone protein htpg
- UniProt
- Q2GFY5
- Pockets
- 7 · best druggability 0.78
Structure
1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 637 | 41% helix, 19% strand | Q2GFY5 |
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 | 274 | 0.78 | 0.90 | 41 | empty |
| 2 | 79 | 0.56 | 0.87 | 20 | empty |
| 3 | 306 | 0.52 | 0.74 | 39 | empty |
| 4 | 55 | 0.36 | 0.79 | 12 | empty |
| 5 | 64 | 0.29 | 0.74 | 12 | 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 Q2GFY5
- Elsewhere: UniProt Q2GFY5 · AlphaFold DB Q2GFY5
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