Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q1AXL4)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q1AXL4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1AXL4
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x166774432Fa02840CA63277F9d861DcB92479204
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- Q1AXL4
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 172 | 43% helix, 22% strand | Q1AXL4 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.50 | 0.81 | 23 | empty |
| 2 | 119 | 0.45 | 0.78 | 28 | empty |
| 3 | 61 | 0.29 | 0.74 | 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 Q1AXL4
- Elsewhere: UniProt Q1AXL4 · AlphaFold DB Q1AXL4
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