Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q728G0)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q728G0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q728G0
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Chaperone protein htpg
- UniProt
- Q728G0
- Pockets
- 11 · best druggability 0.76
Structure
1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 637 | 44% helix, 18% strand | Q728G0 |
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.76 | 0.88 | 48 | empty |
| 2 | 172 | 0.57 | 0.81 | 33 | empty |
| 3 | 118 | 0.48 | 0.80 | 16 | empty |
| 4 | 133 | 0.47 | 0.78 | 18 | empty |
| 5 | 69 | 0.44 | 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 Q728G0
- Elsewhere: UniProt Q728G0 · AlphaFold DB Q728G0
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