› 3ngu

X-ray diffraction
2.29Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoside diphosphate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 16.66 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9U1E1 (Residues: 1-151; Coverage: 100%)
Gene names: L1648.07, LMJF_32_2950
Sequence domains: Nucleoside diphosphate kinase
Structure domains: Nucleoside diphosphate kinase-like domain

Ligands and Environments

1 bound ligand:
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: R32
Unit cell:
a: 123.213Å b: 123.213Å c: 137.983Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.216 0.283
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Recent developments in drug discovery for leishmaniasis and human African trypanosomiasis.
Nagle et al. (2014)
4 more

2 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)
1 more