Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (P61186)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (P61186) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P61186
- Type
- protein
- Length
- 644 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Chaperone protein htpg
- UniProt
- P61186
- Pockets
- 10 · best druggability 0.76
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 644 | 41% helix, 22% strand | P61186 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 778 | 0.76 | 0.80 | 82 | empty |
| 2 | 265 | 0.70 | 0.85 | 40 | empty |
| 3 | 116 | 0.47 | 0.79 | 21 | empty |
| 4 | 66 | 0.44 | 0.82 | 14 | empty |
| 5 | 154 | 0.43 | 0.75 | 29 | 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 P61186
- Elsewhere: UniProt P61186 · AlphaFold DB P61186
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