Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (A7ZXD1)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (A7ZXD1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7ZXD1
- Type
- protein
- Length
- 624 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x02df3F8069b24076E54c06706a40f151233Ec8EE
- Molecule
- Chaperone protein htpg
- UniProt
- A7ZXD1
- Pockets
- 7 · best druggability 0.79
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 624 | 43% helix, 21% strand | A7ZXD1 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 746 | 0.79 | 0.83 | 65 | empty |
| 2 | 85 | 0.43 | 0.79 | 18 | empty |
| 3 | 83 | 0.38 | 0.77 | 14 | empty |
| 4 | 95 | 0.36 | 0.75 | 19 | empty |
| 5 | 50 | 0.33 | 0.79 | 13 | 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 A7ZXD1
- Elsewhere: UniProt A7ZXD1 · AlphaFold DB A7ZXD1
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