› 1n28

X-ray diffraction
1.5Å resolution

Crystal structure of the H48Q mutant of human group IIA phospholipase A2

Released:
DOI: 10.2210/pdb1n28/pdb
PDB entry 1n28 coloured by chain, front view.
PDB entry 1n28 coloured by chain, side view.
PDB entry 1n28 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the H48Q active site mutant of human group IIA secreted phospholipase A2 at 1.5 A resolution provides an insight into the catalytic mechanism.
Edwards SH, Thompson D, Baker SF, Wood SP, Wilton DC
Biochemistry 41 15468-76 (2002)
PMID: 12501175

Function and Biology Details

Reaction catalysed: 
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146964 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2, membrane associated Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 13.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14555 (Residues: 21-144; Coverage: 100%)
Gene names: PLA2B, PLA2G2A, PLA2L, RASF-A
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 119.58Å b: 34.42Å c: 73.9Å
α: 90° β: 126.56° γ: 90°
R-values:
R R work R free
0.184 0.184 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Secretory phospholipase A2 enzymes as pharmacological targets for treatment of disease.
Quach et al. (2014)
4 more

4 mentions without citation

Structural and Functional Aspects of Targeting the Secreted Human Group IIA Phospholipase A2.
Kim et al. (2020)
3 more