1e7w

X-ray diffraction
1.75Å resolution

One active site, two modes of reduction correlate the mechanism of leishmania pteridine reductase with pterin metabolism and antifolate drug resistance in trpanosomes

Released:

Function and Biology Details

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

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
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 30.72 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
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 NDP 2 x NDP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21212
Unit cell:
a: 80.312Å b: 80.8Å c: 90.747Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.244
Expression system: Escherichia coli