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tRNA-Guanine Transglycosylase (TGT) in co-crystallized complex with (E)-N-ethyl-4-oxo-4-phenylbut-2-enamide

Analyse tRNA-Guanine Transglycosylase (TGT) in co-crystallized complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YGV
Type
protein
Length
367 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.63
Source
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Molecule
Queuine tRNA-ribosyltransferase
EC
2.4.2.29
UniProt
P28720
Ligands
OQH, ZN
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · resolution 1.63 · 1 distinct chain · 47% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AQueuine tRNA-ribosyltransferase (EC 2.4.2.29)protein36747% helix, 18% strandP28720

Ligands and binding sites

  • OQH · ~{N}-ethyl-4-oxidanylidene-4-phenyl-butanamide · ligand · chains A
  • ZN · Zinc ion · metal · chains A
  • GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12800.660.8245GOL
2760.410.7914empty
3780.390.7719empty
4600.340.7812empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 6YGV · TRNA-guanine transglycosylase (tgt) in co-crystallized complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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