Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (O33012)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (O33012) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O33012
- Type
- protein
- Length
- 656 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Chaperone protein htpg
- UniProt
- O33012
- Pockets
- 10 · best druggability 0.77
Structure
1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 656 | 40% helix, 21% strand | O33012 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 470 | 0.77 | 0.85 | 61 | empty |
| 2 | 326 | 0.74 | 0.86 | 56 | empty |
| 3 | 224 | 0.55 | 0.78 | 33 | empty |
| 4 | 180 | 0.51 | 0.78 | 25 | empty |
| 5 | 204 | 0.49 | 0.76 | 24 | 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 O33012
- Elsewhere: UniProt O33012 · AlphaFold DB O33012
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