Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (P9WMJ6)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (P9WMJ6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P9WMJ6
- Type
- protein
- Length
- 647 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Chaperone protein htpg
- UniProt
- P9WMJ6
- Pockets
- 9 · best druggability 0.76
Structure
1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 647 | 41% helix, 21% strand | P9WMJ6 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 756 | 0.76 | 0.80 | 83 | empty |
| 2 | 96 | 0.72 | 0.95 | 25 | empty |
| 3 | 248 | 0.61 | 0.80 | 37 | empty |
| 4 | 205 | 0.55 | 0.79 | 28 | empty |
| 5 | 101 | 0.40 | 0.76 | 20 | 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 P9WMJ6
- Elsewhere: UniProt P9WMJ6 · AlphaFold DB P9WMJ6
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