Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (C1AY15)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (C1AY15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C1AY15
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- C1AY15
- Pockets
- 1 · best druggability 0.35
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 190 | 41% helix, 23% strand | C1AY15 |
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 | 62 | 0.35 | 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 C1AY15
- Elsewhere: UniProt C1AY15 · AlphaFold DB C1AY15
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