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Crystal structure of tryptophanyl-tRNA synthetase (ec 6.1.1.2) (tryptophan-tRNA LIGASE)(TRPRS) (TM0492) from thermotoga maritima at 2.50 a resolution

Analyse Crystal structure of tryptophanyl-tRNA synthetase (ec 6.1.1.2) (tryptophan-tRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2G36
Type
protein
Length
322 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophanyl-tRNA synthetase
EC
6.1.1.2
UniProt
Q9WYW2
Ligands
SF4, TRP
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATryptophanyl-tRNA synthetase (EC 6.1.1.2)protein32257% helix, 8% strandQ9WYW2

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · chains A
  • TRP · Tryptophan · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16120.700.7851TRP
2530.290.7513empty

Compared structures

  • 2G36 · Crystal structure of Tryptophanyl-tRNA synthetase (EC 6.1.1.2) (Tryptophan-tRNA… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WYW2 · AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase (Q9WYW2) · a predicted model of the same protein · chain A against A, TM-score 0.99

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