› 1le6

X-ray diffraction
1.97Å resolution

CARBOXYLIC ESTER HYDROLASE, P 1 21 1 SPACE GROUP

Released:
DOI: 10.2210/pdb1le6/pdb
PDB entry 1le6 coloured by chain, front view.
PDB entry 1le6 coloured by chain, side view.
PDB entry 1le6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes.
Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ
J Biol Chem 277 29086-93 (2002)
PMID: 12161451

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-127495 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Group 10 secretory phospholipase A2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 123 amino acids
Theoretical weight: 13.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15496 (Residues: 43-165; Coverage: 92%)
Gene name: PLA2G10
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

2 bound ligands:
Ligand CA 3 x CA
Ligand MPD 3 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 51.173Å b: 62.134Å c: 70.368Å
α: 90° β: 99.35° γ: 90°
R-values:
R R work R free
0.192 0.19 0.231
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.
Dennis et al. (2011)
14 more

6 mentions without citation

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