› 2bbf

X-ray diffraction
1.7Å resolution

Crystal structure of tRNA-guanine transglycosylase (TGT) from Zymomonas mobilis in complex with 6-amino-3,7-dihydro-imidazo[4,5-g]quinazolin-8-one

Released:
DOI: 10.2210/pdb2bbf/pdb
PDB entry 2bbf coloured by chain, front view.
PDB entry 2bbf coloured by chain, side view.
PDB entry 2bbf coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate binding.
Stengl B, Meyer EA, Heine A, Brenk R, Diederich F, Klebe G
J Mol Biol 370 492-511 (2007)
PMID: 17524419

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: 386 amino acids
Theoretical weight: 42.93 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28720 (Residues: 1-386; Coverage: 100%)
Gene names: ZMO0363, tgt
Sequence domains: Queuine tRNA-ribosyltransferase
Structure domains: Queuine tRNA-ribosyltransferase-like

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand 344 1 x 344
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 91.2Å b: 65.59Å c: 69.81Å
α: 90° β: 96.07° γ: 90°
R-values:
R R work R free
0.196 0.196 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

A medicinal chemist's guide to molecular interactions.
Bissantz et al. (2010)
8 more

2 mentions without citation

CSAR benchmark exercise of 2010: selection of the protein-ligand complexes.
Dunbar et al. (2011)
1 more