› 2x9n

X-ray diffraction
1.15Å resolution

High resolution structure of TbPTR1 in complex with cyromazine

Released:
DOI: 10.2210/pdb2x9n/pdb
PDB entry 2x9n coloured by chain, front view.
PDB entry 2x9n coloured by chain, side view.
PDB entry 2x9n coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
High-resolution structures of Trypanosoma brucei pteridine reductase ligand complexes inform on the placement of new molecular entities in the active site of a potential drug target.
Dawson A, Tulloch LB, Barrack KL, Hunter WN
Acta Crystallogr D Biol Crystallogr 66 1334-40 (2010)
PMID: 21123874

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-131227 (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
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
5 bound ligands:
Ligand AX3 4 x AX3
Ligand DTD 2 x DTD
Ligand NA 2 x NA
Ligand D1D 2 x D1D
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 74.5Å b: 90Å c: 82.4Å
α: 90° β: 115.5° γ: 90°
R-values:
R R work R free
0.126 not available 0.152
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)
7 other articles

3 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)
2 more