MolNFT v1 · #180172 · protein
AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q12PB2)
Q12PB2: “AlphaFold monomer V2.0 prediction for chaperone protein htpg (Q12PB2)”. 6 pockets (best druggability 0.76). MolNFT v1 #180172 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q12PB2
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x199F2372C81Df58575EBEe1A02acd194D122F06F
- Molecule
- Chaperone protein htpg
- UniProt
- Q12PB2
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 637 | 43% helix, 20% strand | Q12PB2 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1049 | 0.76 | 0.79 | 88 | empty |
| 2 | 73 | 0.52 | 0.85 | 20 | empty |
| 3 | 157 | 0.48 | 0.77 | 31 | empty |
| 4 | 122 | 0.46 | 0.78 | 21 | empty |
| 5 | 68 | 0.32 | 0.75 | 16 | 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 Q12PB2
- Elsewhere: UniProt Q12PB2 · AlphaFold DB Q12PB2
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