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AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (P13188)

Analyse AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (P13188) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P13188
Type
protein
Length
809 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xDc7b11bC19E7871dc4cc7f885eEd3e0D4eBdc448
Molecule
Glutamine--tRNA ligase
UniProt
P13188
Pockets
5 · best druggability 0.67

Structure

1 distinct chain · 39% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamine--tRNA ligaseprotein80939% helix, 18% strandP13188

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13730.670.8039empty
22780.610.8044empty
31060.460.7915empty
4930.380.7615empty
5500.280.7513empty

Compared structures

  • 4H3S · The Structure of Glutaminyl-tRNA Synthetase from Saccharomyces Cerevisiae · an experimental structure of the same protein · chain A against A, TM-score 0.71
  • 4H3S · The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae · an experimental structure of the same protein · chain A against A, TM-score 0.71
  • 3TL4 · Crystal Structure of the tRNA Binding Domain of Glutaminyl-tRNA Synthetase from… · an experimental structure of the same protein · chain A against X, TM-score 0.22
  • 3TL4 · Crystal structure of the tRNA binding domain of glutaminyl-tRNA synthetase from… · an experimental structure of the same protein · chain A against X, TM-score 0.22

Analyse

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