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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.65 Å)

Structure validation