Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q65RV7)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q65RV7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q65RV7
- Type
- protein
- Length
- 626 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x537a7697cdcd278751bf40d02a88e497634048D7
- Molecule
- Chaperone protein htpg
- UniProt
- Q65RV7
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 626 | 43% helix, 20% strand | Q65RV7 |
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 | 826 | 0.76 | 0.80 | 73 | empty |
| 2 | 93 | 0.52 | 0.83 | 20 | empty |
| 3 | 233 | 0.51 | 0.76 | 28 | empty |
| 4 | 128 | 0.43 | 0.76 | 20 | empty |
| 5 | 81 | 0.31 | 0.73 | 16 | 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 Q65RV7
- Elsewhere: UniProt Q65RV7 · AlphaFold DB Q65RV7
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