Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A1VDR1)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A1VDR1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1VDR1
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- A1VDR1
- Pockets
- 1 · best druggability 0.35
Structure
1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 201 | 44% helix, 21% strand | A1VDR1 |
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 | 83 | 0.35 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 A1VDR1
- Elsewhere: UniProt A1VDR1 · AlphaFold DB A1VDR1
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