Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B0B927)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B0B927) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0B927
- Type
- protein
- Length
- 179 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf562F10F7328F0E98474bd83C5fD20dd558c7ed6
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- B0B927
- Pockets
- 2 · best druggability 0.37
Structure
1 distinct chain · 42% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 179 | 42% helix, 25% strand | B0B927 |
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 | 70 | 0.37 | 0.78 | 18 | empty |
| 2 | 50 | 0.25 | 0.73 | 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 B0B927
- Elsewhere: UniProt B0B927 · AlphaFold DB B0B927
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