› 7sb7

X-ray diffraction
2.65Å resolution

Crystal structure of T. brucei hypoxanthine guanine phosphoribosyltransferase in complex with (4S,7S)-7-hydroxy-4-((guanin-9-yl)methyl)-2,5-dioxaheptan-1,7-diphosphonate

Released:
DOI: 10.2210/pdb7sb7/pdb
PDB entry 7sb7 coloured by chain, front view.
PDB entry 7sb7 coloured by chain, side view.
PDB entry 7sb7 coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Stereo-Defined Acyclic Nucleoside Phosphonates are Selective and Potent Inhibitors of Parasite 6-Oxopurine Phosphoribosyltransferases.
Klejch T, Keough DT, King G, Doleželová E, Česnek M, Buděšínský M, Zíková A, Janeba Z, Guddat LW, Hocková D
J Med Chem 65 4030-4057 (2022)
PMID: 35175749

Function and Biology Details

Reaction catalysed: 
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hypoxanthine-guanine phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 24.22 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07010 (Residues: 1-210; Coverage: 100%)
Gene name: HGPRT
Sequence domains: Phosphoribosyl transferase domain

Ligands and Environments

1 bound ligand:
Ligand 8QI 2 x 8QI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: C2
Unit cell:
a: 115.908Å b: 93.983Å c: 44.274Å
α: 90° β: 109.125° γ: 90°
R-values:
R R work R free
0.202 0.196 0.253
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Kinetic and Structural Characterization of Trypanosoma cruzi Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferases and Repurposing of Transition-State Analogue Inhibitors.
Glockzin et al. (2023)