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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B7J502)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B7J502) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B7J502
Type
protein
Length
189 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x1991a6b734E5275233F4E0c675B7e48254988D57
Molecule
Peptidyl-tRNA hydrolase
UniProt
B7J502
Pockets
1 · best druggability 0.43

Structure

1 distinct chain · 43% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein18943% helix, 22% strandB7J502

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11010.430.7828empty

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