1c1j

STRUCTURE OF CADMIUM-SUBSTITUTED PHOSPHOLIPASE A2 FROM AGKISTRONDON HALYS PALLAS AT 2.8 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1c1j, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1c1j is a 4 chain structure with sequence from Gloydius halys. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: BOG, CD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PA2BB_GLOHA Snake venom phospholipase A2 (PLA2) that shows potent hemolytic activity, and exhibits medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 90 nM). It is one of the few phospholipases A2 capable of hydrolyzing the phospholipids of E.coli membranes in the presence of a bactericidal/permeability-increasing protein (BPI) of neutrophils. 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. See Also Phospholipase A2 3D structures

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