› 1le7

X-ray diffraction
2.09Å resolution

CARBOXYLIC ESTER HYDROLASE, C 2 2 21 space group

Released:
DOI: 10.2210/pdb1le7/pdb
PDB entry 1le7 coloured by chain, front view.
PDB entry 1le7 coloured by chain, side view.
PDB entry 1le7 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
Molecule details ›
Chains: A, B
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 2 x CA
Ligand MPD 5 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2221
Unit cell:
a: 139.058Å b: 145.098Å c: 28.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.211 0.252
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

2 mentions without citation

Secretory Phospholipases A2, from Snakebite Envenoming to a Myriad of Inflammation Associated Human Diseases-What Is the Secret of Their Activity?
Tonello F. (2023)
1 more