PDBe 3elo

X-ray diffraction
1.55Å resolution

Crystal Structure of Human Pancreatic Prophospholipase A2

Released:
Source organism: Homo sapiens
Primary publication:
Structural insight into the activation mechanism of human pancreatic prophospholipase A2.
J. Biol. Chem. 284 16659-66 (2009)
PMID: 19297324

Function and Biology Details

Reaction catalysed:
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2 Chain: A
Molecule details ›
Chain: A
Length: 133 amino acids
Theoretical weight: 14.87 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P04054 (Residues: 16-148; Coverage: 100%)
Gene names: PLA2, PLA2A, PLA2G1B, PPLA2
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCED ULTRA
Spacegroup: P63
Unit cell:
a: 56.549Å b: 56.549Å c: 60.631Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.145 0.183
Expression system: Komagataella pastoris