Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B5YG54)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B5YG54) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YG54
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- B5YG54
- Pockets
- 1 · best druggability 0.40
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 187 | 41% helix, 23% strand | B5YG54 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.40 | 0.78 | 20 | 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 B5YG54
- Elsewhere: UniProt B5YG54 · AlphaFold DB B5YG54
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