› 1e92

X-ray diffraction
2.2Å resolution

Pteridine reductase 1 from Leishmania major complexed with NADP+ and dihydrobiopterin

Released:
DOI: 10.2210/pdb1e92/pdb
PDB entry 1e92 coloured by chain, front view.
PDB entry 1e92 coloured by chain, side view.
PDB entry 1e92 coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites.
Gourley DG, Schüttelkopf AW, Leonard GA, Luba J, Hardy LW, Beverley SM, Hunter WN
Nat Struct Biol 8 521-5 (2001)
PMID: 11373620

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169629 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pteridine reductase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 288 amino acids
Theoretical weight: 30.44 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q01782 (Residues: 1-288; Coverage: 100%)
Gene names: HMTXR, L1063.01, LmjF23.0270, LmjF_23_0270, PTR1
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
2 bound ligands:
Ligand HBI 4 x HBI
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 94.338Å b: 103.801Å c: 137.412Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Short-chain dehydrogenases/reductases (SDR): the 2002 update.
Oppermann et al. (2003)
5 more

7 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)
6 more