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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q131M0)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q131M0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q131M0
Type
protein
Length
207 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xB797235589280D92Ce4bA47be78Fa8180f655a40
Molecule
Peptidyl-tRNA hydrolase
UniProt
Q131M0
Pockets
1 · best druggability 0.45

Structure

1 distinct chain · 45% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein20745% helix, 21% strandQ131M0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1810.450.8118empty

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