Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q1CZI7)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q1CZI7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1CZI7
- Type
- protein
- Length
- 654 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x68C50954adA417a9303e7cEcfC2b256525160CC6
- Molecule
- Chaperone protein htpg
- UniProt
- Q1CZI7
- Pockets
- 7 · best druggability 0.76
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 654 | 42% helix, 21% strand | Q1CZI7 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.76 | 0.80 | 65 | empty |
| 2 | 98 | 0.60 | 0.87 | 20 | empty |
| 3 | 135 | 0.52 | 0.81 | 18 | empty |
| 4 | 53 | 0.51 | 0.87 | 19 | empty |
| 5 | 169 | 0.48 | 0.77 | 25 | 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 Q1CZI7
- Elsewhere: UniProt Q1CZI7 · AlphaFold DB Q1CZI7
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