› 4br7

X-ray diffraction
1.8Å resolution

Legionella pneumophila NTPDase1 crystal form I, open, AMPNP complex

Released:
DOI: 10.2210/pdb4br7/pdb
PDB entry 4br7 coloured by chain, front view.
PDB entry 4br7 coloured by chain, side view.
PDB entry 4br7 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 Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 41.54 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5ZUA2 (Residues: 37-393; Coverage: 91%)
Gene name: lpg1905
Sequence domains: GDA1/CD39 (nucleoside phosphatase) family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand AU1 1 x AU1
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P321
Unit cell:
a: 102.853Å b: 102.853Å c: 74.779Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.163 0.209
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

Co-localization and confinement of ecto-nucleotidases modulate extracellular adenosine nucleotide distributions.
Rahmaninejad et al. (2020)