› 5l42

X-ray diffraction
2.1Å resolution

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 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: 30.46 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 NDP 4 x NDP
5 bound ligands:
Ligand 6J6 4 x 6J6
Ligand GOL 6 x GOL
Ligand ACT 4 x ACT
Ligand PGE 1 x PGE
Ligand EDO 5 x EDO
1 modified residue:
Ligand CSX 4 x CSX

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 94.699Å b: 104.19Å c: 137.042Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

An Overview on the Therapeutics of Neglected Infectious Diseases-Leishmaniasis and Chagas Diseases.
J et al. (2021)
1 more

2 mentions without citation

Chroman-4-One Derivatives Targeting Pteridine Reductase 1 and Showing Anti-Parasitic Activity.
Di Pisa et al. (2017)
1 more