7INS

STRUCTURE OF PORCINE INSULIN COCRYSTALLIZED WITH CLUPEINE Z

Summary for 7INS

• Entry DOI: 10.2210/pdb7ins/pdb
• Descriptor: INSULIN (CHAIN A), INSULIN (CHAIN B), GENERAL PROTAMINE CHAIN, ... (7 entities in total)
• Functional Keywords: hormone
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted: P01315 P01315
• Total number of polymer chains: 7
• Total formula weight: 19338.63

Authors

Balschmidt, P.,Hansen, F.B.,Dodson, E.,Dodson, G.,Korber, F. (deposition date: 1991-09-03, release date: 1994-01-31, Last modification date: 2025-02-12)

Primary citation

Balschmidt, P.,Hansen, F.B.,Dodson, E.J.,Dodson, G.G.,Korber, F.
Structure of porcine insulin cocrystallized with clupeine Z.
Acta Crystallogr.,Sect.B, 47:975-986, 1991

PubMed Abstract: 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.

PubMed: 1772633
DOI: 10.1107/S010876819100842X

Experimental method

X-RAY DIFFRACTION (2 Å)