› 4brk

X-ray diffraction
1.5Å resolution

Legionella pneumophila NTPDase1 N302Y variant crystal form III (closed) in complex with MG UMPPNP

Released:
DOI: 10.2210/pdb4brk/pdb
PDB 4brk coloured by chain and viewed from the front.
PDB 4brk coloured by chain and viewed from the side.
PDB 4brk coloured by chain and viewed from the top.
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 (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)
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: 41.93 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

5 bound ligands:
Ligand UNP 2 x UNP
Ligand MG 2 x MG
Ligand MES 2 x MES
Ligand GOL 2 x GOL
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.3
Spacegroup: P212121
Unit cell:
a: 80.6Å b: 82.967Å c: 109.578Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.129 0.178
Expression system: Escherichia coli

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Citations

5 review citations

Ectonucleoside triphosphate diphosphohydrolases and ecto-5'-nucleotidase in purinergic signaling: how the field developed and where we are now.
Zimmermann H. (2021)
4 more