1NES

STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION

Summary for 1NES

• Entry DOI: 10.2210/pdb1nes/pdb
• Descriptor: ELASTASE, ACETYL-ALA-PRO-ALA, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: serine protease/inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Sus scrofa (pig)
• Cellular location: Secreted: P00772
• Total number of polymer chains: 3
• Total formula weight: 26630.82

Authors

Meyer Junior, E.F.,Radhakrishnan, R.,M Cole, G.,Presta, L.G. (deposition date: 1995-07-31, release date: 1996-01-29, Last modification date: 2024-10-30)

Primary citation

Meyer Jr., E.F.,Radhakrishnan, R.,Cole, G.M.,Presta, L.G.
Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 A resolution.
J.Mol.Biol., 189:533-539, 1986

PubMed Abstract: A single crystal of porcine pancreatic elastase was mounted in a thin-walled capillary and allowed to react with acetyl-Ala-Pro-Ala-paranitroanalide. Diffraction data to 1.65 A resolution were measured and the isomorphous structure was solved from the difference Fourier map. The structure contains two surprises. Two molecules of the product: acetyl-Ala-Pro-Ala molecule are bound in the extended binding site. Both molecules are bound backwards with respect to the established mode of peptide binding.

PubMed: 3640831
DOI: 10.1016/0022-2836(86)90322-0

Experimental method

X-RAY DIFFRACTION (1.65 Å)