› 2xox

X-ray diffraction
2.5Å resolution

Crystal structure of pteridine reductase (PTR1) from Leishmania donovani

Released:
DOI: 10.2210/pdb2xox/pdb
PDB entry 2xox coloured by chain, front view.
PDB entry 2xox coloured by chain, side view.
PDB entry 2xox coloured by chain, top view.
Source organism: Leishmania donovani
Primary publication:
Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site.
Barrack KL, Tulloch LB, Burke LA, Fyfe PK, Hunter WN
OpenAccess logo Acta Crystallogr Sect F Struct Biol Cryst Commun 67 33-7 (2011)
PMID: 21206018

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180254 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pteridine reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 30.28 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6QDB5 (Residues: 1-288; Coverage: 100%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2221
Unit cell:
a: 107.509Å b: 126.443Å c: 87.513Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Structure and dynamics of pteridine reductase 1: the key phenomena relevant to enzyme function and drug design.
Panecka-Hofman et al. (2023)
6 other articles

12 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
11 more