1ddx

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spinqualitylabelsall models 1ddx, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A MIXTURE OF ARACHIDONIC ACID AND PROSTAGLANDIN BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2: PROSTAGLANDIN STRUCTURE

Overview

Cyclooxygenases are bifunctional enzymes that catalyse the first committed, step in the synthesis of prostaglandins, thromboxanes and other, eicosanoids. The two known cyclooxygenases isoforms share a high degree of, amino-acid sequence similarity, structural topology and an identical, catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential, reactions in spatially distinct, but mechanistically coupled active sites., The initial cyclooxygenase reaction converts arachidonic acid (which is, achiral) to prostaglandin G2 (which has five chiral centres). The, subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin, H2. Here we report the co-crystal structures of murine, apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin., These structures suggest the molecular basis for the stereospecificity of, prostaglandin G2 synthesis.

About this Structure

1DDX is a Single protein structure of sequence from Mus musculus with NAG, BOG and PGX as ligands. Active as Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1 Full crystallographic information is available from OCA.

Reference

Structural insights into the stereochemistry of the cyclooxygenase reaction., Kiefer JR, Pawlitz JL, Moreland KT, Stegeman RA, Hood WF, Gierse JK, Stevens AM, Goodwin DC, Rowlinson SW, Marnett LJ, Stallings WC, Kurumbail RG, Nature. 2000 May 4;405(6782):97-101. PMID:10811226

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