4APE

THE ACTIVE SITE OF ASPARTIC PROTEINASES

「2APE」から置き換えられました 「1APE」から置き換えられました

4APE の概要

• エントリーDOI: 10.2210/pdb4ape/pdb
• 分子名称: ENDOTHIAPEPSIN (2 entities in total)
• 機能のキーワード: hydrolase (acid proteinase)
• 由来する生物種: Cryphonectria parasitica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33813.86

構造登録者

Pearl, L.H.,Sewell, B.T.,Jenkins, J.A.,Cooper, J.B.,Blundell, T.L. (登録日: 1986-06-09, 公開日: 1986-07-14, 最終更新日: 2024-10-09)

主引用文献

Pearl, L.,Blundell, T.
The Active Site of Aspartic Proteinases
FEBS Lett., 174:96-101, 1984

PubMed Abstract: The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.

PubMed: 6381096
DOI: 10.1016/0014-5793(84)81085-6

実験手法

X-RAY DIFFRACTION (2.1 Å)