MolNFT v1 · #319398 · protein
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (C3LPI9)
C3LPI9: “AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (C3LPI9)”. 1 pocket (best druggability 0.43). MolNFT v1 #319398 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- C3LPI9
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- C3LPI9
- Pockets
- 1 · best druggability 0.43
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 196 | 43% helix, 22% strand | C3LPI9 |
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 | 92 | 0.43 | 0.79 | 26 | empty |
Compared structures
- 2MJL · Solution structure of peptidyl-tRNA hyrolase from vibrio cholerae · an experimental structure of the same protein · chain A against A, TM-score 0.90
- 2MJL · Solution structure of peptidyl-tRNA hyrolase from Vibrio cholerae · an experimental structure of the same protein · chain A against A, TM-score 0.90
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 C3LPI9
- Elsewhere: UniProt C3LPI9 · AlphaFold DB C3LPI9
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