1NES

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

1NES の概要

• エントリーDOI: 10.2210/pdb1nes/pdb
• 分子名称: ELASTASE, ACETYL-ALA-PRO-ALA, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: serine protease/inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 26630.82

構造登録者

Meyer Junior, E.F.,Radhakrishnan, R.,M Cole, G.,Presta, L.G. (登録日: 1995-07-31, 公開日: 1996-01-29, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.65 Å)