Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (P44516)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (P44516) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P44516
- Type
- protein
- Length
- 626 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x822BfDB52f100Af7414C872a89eE1bfF1069766B
- Molecule
- Chaperone protein htpg
- UniProt
- P44516
- Pockets
- 8 · best druggability 0.75
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 626 | 43% helix, 21% strand | P44516 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 851 | 0.75 | 0.79 | 65 | empty |
| 2 | 69 | 0.56 | 0.88 | 20 | empty |
| 3 | 53 | 0.56 | 0.90 | 25 | empty |
| 4 | 81 | 0.43 | 0.80 | 23 | empty |
| 5 | 94 | 0.43 | 0.78 | 19 | 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 P44516
- Elsewhere: UniProt P44516 · AlphaFold DB P44516
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