1gp7

Acidic Phospholipase A2 from venom of Ophiophagus HannahAcidic Phospholipase A2 from venom of Ophiophagus Hannah

Structural highlights 1gp7 is a 3 chain structure with sequence from Ophiophagus hannah. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PA2A1_OPHHA Snake venom phospholipase A2 (PLA2) that may exhibit cardiotoxicity, myotoxicity, antiplatelet activity, and edema-inducing activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of an acidic phospholipase A(2) from Ophiophagus hannah (king cobra) has been determined by molecular replacement at 2.6-A resolution to a crystallographic R factor of 20.5% (R(free)=23.3%) with reasonable stereochemistry. The venom enzyme contains an unusual "pancreatic loop." The conformation of the loop is well defined and different from those in pancreas PLA(2), showing its structural variability. This analysis provides the first structure of a PLA(2)-type cardiotoxin. The sites related to the cardiotoxic and myotoxic activities are explored and the oligomer observed in the crystalline state is described. Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with the "pancreatic loop".,Zhang HL, Xu SJ, Wang QY, Song SY, Shu YY, Lin ZJ J Struct Biol. 2002 Jun;138(3):207-15. PMID:12217659 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase A2 3D structures

spinqualitylabelsall models 1gp7, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image