› 4brh

X-ray diffraction
1.69Å resolution

Legionella pneumophila NTPDase1 crystal form II (closed) in complex with MG AND THIAMINE PHOSPHOVANADATE

Released:
DOI: 10.2210/pdb4brh/pdb
PDB entry 4brh coloured by chain, front view.
PDB entry 4brh coloured by chain, side view.
PDB entry 4brh coloured by chain, top view.
Source organism: Legionella pneumophila
Primary publication:
Crystallographic snapshots along the reaction pathway of nucleoside triphosphate diphosphohydrolases.
Zebisch M, Krauss M, Schäfer P, Lauble P, Sträter N
Structure 21 1460-75 (2013)
PMID: 23830739

Function and Biology Details

Reaction catalysed: 
(1a) a nucleoside 5'-triphosphate + H(2)O = a nucleoside 5'-diphosphate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ectonucleoside triphosphate diphosphohydrolase I Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 41.88 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5ZUA2 (Residues: 35-393; Coverage: 91%)
Gene name: lpg1905
Sequence domains: GDA1/CD39 (nucleoside phosphatase) family
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand TMV 2 x TMV
Ligand MG 2 x MG
Ligand MES 2 x MES
Ligand DVT 2 x DVT
Ligand CL 2 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 62.435Å b: 85.759Å c: 72.306Å
α: 90° β: 106.44° γ: 90°
R-values:
R R work R free
0.16 0.159 0.192
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Therapeutic potentials of ecto-nucleoside triphosphate diphosphohydrolase, ecto-nucleotide pyrophosphatase/phosphodiesterase, ecto-5'-nucleotidase, and alkaline phosphatase inhibitors.
al-Rashida et al. (2014)
3 more

3 mentions without citation

The use of polyoxometalates in protein crystallography - An attempt to widen a well-known bottleneck.
Bijelic et al. (2015)
2 more