Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B2JA15)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B2JA15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2JA15
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE44BC5A672E798FFA7bFD27127EF616fEF8330bB
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- B2JA15
- Pockets
- 2 · best druggability 0.47
Structure
1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 213 | 42% helix, 19% strand | B2JA15 |
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 | 162 | 0.47 | 0.77 | 29 | empty |
| 2 | 108 | 0.38 | 0.75 | 21 | 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 B2JA15
- Elsewhere: UniProt B2JA15 · AlphaFold DB B2JA15
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