› 1oxw

X-ray diffraction
2.2Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Patatin-17 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 373 amino acids
Theoretical weight: 41.87 KDa
Source organism: Solanum cardiophyllum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8LPW4 (Residues: 23-386; Coverage: 100%)
Sequence domains: Patatin-like phospholipase
Structure domains: Cytosolic phospholipase A2 catalytic domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 39 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2221
Unit cell:
a: 97.18Å b: 171.42Å c: 129.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.272
Expression system: Escherichia coli

Quick links

Citations

43 review citations

FAT SIGNALS--lipases and lipolysis in lipid metabolism and signaling.
Zechner et al. (2012)
42 more

26 mentions without citation

Using hydrogen/deuterium exchange mass spectrometry to define the specific interactions of the phospholipase A2 superfamily with lipid substrates, inhibitors, and membranes.
Cao et al. (2013)
25 more