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Crystal structure of human T2-tryptophanyl-tRNA synthetase with H130R mutation

Analyse Crystal structure of human T2-tryptophanyl-tRNA synthetase with H130R mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5UJI
Type
protein
Length
710 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophan--tRNA ligase, cytoplasmic
EC
6.1.1.2
UniProt
P23381
Pockets
9 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2)protein35652% helix, 9% strandP23381
BTryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2)protein35457% helix, 8% strandP23381

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16740.760.8151empty
24590.700.8133empty
32620.610.8028empty
4780.590.8818empty
51400.530.8117empty

Interfaces

1 interface between chains.

  • A–B · 1612 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 5UJI · Crystal structure of human T2-Tryptophanyl-tRNA synthetase with H130R mutation · the same entry in another collection · chain A against A, TM-score 1.00
  • P23381 · AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase, cytoplasmic (P23381) · a predicted model of the same protein · chain B against A, TM-score 0.86

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