PDBe 1s18

X-ray diffraction
1.7Å resolution

Structure and protein design of human apyrase

Released:
Source organism: Homo sapiens
Primary publication:
Structure and protein design of a human platelet function inhibitor.
Cell 116 649-59 (2004)
PMID: 15006348

Function and Biology Details

Reaction catalysed:
A nucleoside diphosphate + H(2)O = a nucleoside phosphate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble calcium-activated nucleotidase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 37.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WVQ1 (Residues: 71-401; Coverage: 83%)
Gene names: CANT1, SHAPY
Sequence domains: Apyrase
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 43.163Å b: 52.501Å c: 77.925Å
α: 99.44° β: 106.58° γ: 99.89°
R-values:
R R work R free
0.159 0.157 0.191
Expression system: Escherichia coli