Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q1JEA1)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q1JEA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1JEA1
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF4Ae8661cb075C3a3cDb0e439E3Eef84872a1286
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- Q1JEA1
- Pockets
- 1 · best druggability 0.31
Structure
1 distinct chain · 42% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 189 | 42% helix, 25% strand | Q1JEA1 |
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 | 51 | 0.31 | 0.77 | 15 | 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 Q1JEA1
- Elsewhere: UniProt Q1JEA1 · AlphaFold DB Q1JEA1
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