Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q92F62)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q92F62) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92F62
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf635025d4b71bb1581df1a0b5A5a5eC99823AA86
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- Q92F62
- Pockets
- 2 · best druggability 0.38
Structure
1 distinct chain · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 184 | 42% helix, 26% strand | Q92F62 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.38 | 0.76 | 20 | empty |
| 2 | 50 | 0.28 | 0.75 | 12 | 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 Q92F62
- Elsewhere: UniProt Q92F62 · AlphaFold DB Q92F62
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