Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B5XIP6)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B5XIP6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5XIP6
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- B5XIP6
- Pockets
- 1 · best druggability 0.36
Structure
1 distinct chain · 43% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 189 | 43% helix, 25% strand | B5XIP6 |
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 | 60 | 0.36 | 0.78 | 18 | empty |
Compared structures
- 4QT4 · Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium… · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 4QT4 · Crystal structure of peptidyl-tRNA hydrolase from a gram-positive bacterium… · an experimental structure of the same protein · chain A against A, TM-score 0.95
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 B5XIP6
- Elsewhere: UniProt B5XIP6 · AlphaFold DB B5XIP6
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