MolNFT v1 · #180050 · protein
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q5FS51)
Q5FS51: “AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q5FS51)”. 10 pockets (best druggability 0.80). MolNFT v1 #180050 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5FS51
- Type
- protein
- Length
- 623 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x795B30fA999F90F224362808144752F0c0125c76
- Molecule
- Chaperone protein htpg
- UniProt
- Q5FS51
- Pockets
- 10 · best druggability 0.80
Structure
1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 623 | 40% helix, 18% strand | Q5FS51 |
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.80 | 0.94 | 36 | empty |
| 2 | 73 | 0.47 | 0.83 | 18 | empty |
| 3 | 153 | 0.45 | 0.76 | 24 | empty |
| 4 | 88 | 0.42 | 0.78 | 20 | empty |
| 5 | 79 | 0.41 | 0.79 | 14 | 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 Q5FS51
- Elsewhere: UniProt Q5FS51 · AlphaFold DB Q5FS51
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