1UA3

Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

1UA3 の概要

• エントリーDOI: 10.2210/pdb1ua3/pdb
• 関連するPDBエントリー: 1JFH
• 関連するBIRD辞書のPRD_ID: PRD_900001 PRD_900009
• 分子名称: Alpha-amylase, pancreatic, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: beta-alpha-barrels, hydrolase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted, extracellular space: P00690
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57504.58

構造登録者

Payan, F.,Qian, M. (登録日: 2003-02-27, 公開日: 2003-10-14, 最終更新日: 2024-11-13)

主引用文献

Payan, F.,Qian, M.
Crystal Structure of the Pig Pancreatic alpha-Amylase Complexed with Malto-Oligosaccharides
J.PROTEIN CHEM., 22:275-284, 2003

PubMed Abstract: The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites. The electron density region observed at the active site, filling subsites-3 through-1, was interpreted in terms of the process of enzyme-catalyzed hydrolysis undergone by maltopentaose. Because the expected conformational changes in the "flexible loop" that constitutes the surface edge of the active site were not observed, the movement of the loop may depend on aglycone site being filled. The crystal structure was refined at 2.01 A resolution to an R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of 3910 protein atoms, one calcium ion, two chloride ions, 103 oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene glycol atoms.

PubMed: 12962327
DOI: 10.1023/A:1025072520607

実験手法

X-RAY DIFFRACTION (2.01 Å)