Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q2GDR7)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q2GDR7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2GDR7
- Type
- protein
- Length
- 620 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x60b04d6bf0a85B202E181bFDEA50a91FE1d5a458
- Molecule
- Chaperone protein htpg
- UniProt
- Q2GDR7
- Pockets
- 9 · best druggability 0.78
Structure
1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 620 | 38% helix, 20% strand | Q2GDR7 |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.78 | 0.90 | 44 | empty |
| 2 | 63 | 0.46 | 0.84 | 18 | empty |
| 3 | 181 | 0.43 | 0.74 | 23 | empty |
| 4 | 107 | 0.42 | 0.77 | 17 | empty |
| 5 | 102 | 0.41 | 0.76 | 17 | 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 Q2GDR7
- Elsewhere: UniProt Q2GDR7 · AlphaFold DB Q2GDR7
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