5LP1

CRYSTAL STRUCTURE OF HUMAN LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 IN COMPLEX WITH A [1.1.1]BICYCLOPENTANE-CONTAINING INHIBITOR AT 1.91A RESOLUTION.

Summary for 5LP1

Entry DOI	10.2210/pdb5lp1/pdb
Descriptor	Platelet-activating factor acetylhydrolase, CHLORIDE ION, ~{N}-[2-(diethylamino)ethyl]-2-[2-[(4-fluorophenyl)methylsulfanyl]-4-oxidanylidene-5~{H}-cyclopenta[d]pyrimidin-1-yl]-~{N}-[[3-[4-(trifluoromethyl)phenyl]-1-bicyclo[1.1.1]pentanyl]methyl]ethanamide, ... (4 entities in total)
Functional Keywords	plasma platelet-activating factor acetylhydrolase, secreted protein, alpha/beta-hydrolase-fold, ldl-bound; lipoprotein associated phospholipase a2, lp-pla2, group viia pla2, glycoprotein, hydrolase, lipid degradation, polymorphism, secreted, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	44928.80
Authors	Somers, D. (deposition date: 2016-08-11, release date: 2017-02-01, Last modification date: 2019-06-12)
Primary citation	Measom, N.D.,Down, K.D.,Hirst, D.J.,Jamieson, C.,Manas, E.S.,Patel, V.K.,Somers, D.O. Investigation of a Bicyclo[1.1.1]pentane as a Phenyl Replacement within an LpPLA2 Inhibitor. ACS Med Chem Lett, 8:43-48, 2017 Cited by PubMed: 28105273 DOI: 10.1021/acsmedchemlett.6b00281 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.91 Å)

Structure validation