› 2qzr

X-ray diffraction
1.95Å resolution

tRNA-Guanine Transglycosylase(TGT) in Complex with 6-amino-2-[(1-naphthylmethyl)amino]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one

Released:
DOI: 10.2210/pdb2qzr/pdb
PDB entry 2qzr coloured by chain, front view.
PDB entry 2qzr coloured by chain, side view.
PDB entry 2qzr coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
Potent inhibitors of tRNA-guanine transglycosylase, an enzyme linked to the pathogenicity of the Shigella bacterium: charge-assisted hydrogen bonding.
Hörtner SR, Ritschel T, Stengl B, Kramer C, Schweizer WB, Wagner B, Kansy M, Klebe G, Diederich F
Angew Chem Int Ed Engl 46 8266-9 (2007)
PMID: 17902085

Function and Biology Details

Reaction catalysed: 
Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Queuine tRNA-ribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 385 amino acids
Theoretical weight: 42.79 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28720 (Residues: 2-386; Coverage: 100%)
Gene names: ZMO0363, tgt
Sequence domains: Queuine tRNA-ribosyltransferase
Structure domains: Queuine tRNA-ribosyltransferase-like

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand S79 1 x S79
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 88.085Å b: 63.44Å c: 71.123Å
α: 90° β: 93.3° γ: 90°
R-values:
R R work R free
0.198 0.198 0.259
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Molecular recognition in chemical and biological systems.
Persch et al. (2015)
2 more