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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B9J795)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B9J795) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B9J795
Type
protein
Length
238 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
Molecule
Peptidyl-tRNA hydrolase
UniProt
B9J795
Pockets
2 · best druggability 0.35

Structure

1 distinct chain · 42% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein23842% helix, 18% strandB9J795

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1750.350.7617empty
2660.330.7614empty

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