1vl9

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spinqualitylabelsall models 1vl9, resolution 0.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2

Overview

The enzyme phospholipase A2 catalyzes the hydrolysis of the sn-2 acyl, chain of phospholipids, forming fatty acids and lysophospholipids. The, crystal structure of a triple mutant (K53,56,121M) of bovine pancreatic, phospholipase A2 in which the lysine residues at positions 53, 56 and 121, are replaced recombinantly by methionines has been determined at atomic, resolution (0.97 A). The crystal is monoclinic (space group P2), with, unit-cell parameters a = 36.934, b = 23.863, c = 65.931 A, beta = 101.47, degrees. The structure was solved by molecular replacement and has been, refined to a final R factor of 10.6% (Rfree = 13.4%) using 63,926 unique, reflections. The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six, 2-methyl-2,4-pentanediol molecules. The surface-loop residues 60-70 are, ordered and have clear electron density.

About this Structure

1VL9 is a Single protein structure of sequence from Bos taurus with CA, CL, MRD and MPD as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2., Sekar K, Rajakannan V, Gayathri D, Velmurugan D, Poi MJ, Dauter M, Dauter Z, Tsai MD, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):3-7. Epub 2004 Sep 25. PMID:16508077

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