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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q5SHZ2)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q5SHZ2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q5SHZ2
Type
protein
Length
183 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
Molecule
Peptidyl-tRNA hydrolase
UniProt
Q5SHZ2
Pockets
1 · best druggability 0.41

Structure

1 distinct chain · 46% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein18346% helix, 23% strandQ5SHZ2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11030.410.7722empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 8X5T · Crystal structure of Thermus thermophilus peptidyl-tRNA hydrolase in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.98
  • 5ZX8 · Crystal structure of peptidyl-tRNA hydrolase from thermus thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.97
  • 5ZX8 · Crystal structure of peptidyl-tRNA hydrolase from Thermus thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.97
  • 8X5U · Crystal structure of Thermus thermophilus peptidyl-tRNA hydrolase C-terminal 16 amino… · an experimental structure of the same protein · chain A against A, TM-score 0.89

Analyse

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