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TRNA-guanine-transglycosylase (tgt) mutant V262D apo-structure

Analyse TRNA-guanine-transglycosylase (tgt) mutant V262D apo-structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IPP
Type
protein
Length
374 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Queuine tRNA-ribosyltransferase
EC
2.4.2.29
UniProt
P28720
Ligands
ZN
Pockets
2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AQueuine tRNA-ribosyltransferase (EC 2.4.2.29)protein37445% helix, 18% strandP28720

Ligands and binding sites

  • 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12160.650.8437GOL
2550.280.7511empty

Compared structures

  • 4IPP · tRNA-guanine-transglycosylase (TGT) mutant V262D APO-Structure · the same entry in another collection · chain A against A, TM-score 1.00

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