7ins

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7ins, resolution 2.0Å

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STRUCTURE OF PORCINE INSULIN COCRYSTALLIZED WITH CLUPEINE Z

Overview

The crystal structure of NPH-insulin, pig insulin cocrystallized with, zinc, m-cresol and protamine, has been solved by molecular replacement and, refined using restrained least-squares refinement methods. The final, crystallographic R factor for all reflections between 2 and 10 A is 19.4%., The insulin molecules are arranged as hexamers with two tetrahedrally, coordinated Zn atoms in the central channel and one m-cresol bound to each, monomer near His B5. One protamine binding site has been unequivocally, identified near a dimer-dimer interface, although most of the polypeptide, is crystallographically disordered. The conformation of the insulin moiety, and the structural differences between the three unique monomers have been, analysed. The zinc and m-cresol environments are described and the nature, of the protamine binding site is outlined.

About this Structure

7INS is a Protein complex structure of sequences from Sus scrofa with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of porcine insulin cocrystallized with clupeine Z., Balschmidt P, Hansen FB, Dodson EJ, Dodson GG, Korber F, Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):975-86. PMID:1772633

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