Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A0RMV6)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A0RMV6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0RMV6
- Type
- protein
- Length
- 181 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- A0RMV6
- Pockets
- 2 · best druggability 0.41
Structure
1 distinct chain · 45% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 181 | 45% helix, 23% strand | A0RMV6 |
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 | 83 | 0.41 | 0.79 | 24 | empty |
| 2 | 66 | 0.31 | 0.75 | 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 A0RMV6
- Elsewhere: UniProt A0RMV6 · AlphaFold DB A0RMV6
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