› 6rx0

X-ray diffraction
1.2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pteridine reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 288 amino acids
Theoretical weight: 30.67 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O76290 (Residues: 1-268; Coverage: 100%)
Gene name: PTR1
Sequence domains: Enoyl-(Acyl carrier protein) reductase

Ligands and Environments

4 bound ligands:
Ligand NAP 4 x NAP
Ligand ACT 1 x ACT
Ligand KM5 3 x KM5
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 74.854Å b: 90.502Å c: 82.951Å
α: 90° β: 115.77° γ: 90°
R-values:
R R work R free
0.129 0.128 0.152
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Current Treatments to Control African Trypanosomiasis and One Health Perspective.
Venturelli et al. (2022)
2 more

1 mention without citation

Multitarget, Selective Compound Design Yields Potent Inhibitors of a Kinetoplastid Pteridine Reductase 1.
Pöhner et al. (2022)