4ER2

The active site of aspartic proteinases

4ER2 の概要

• エントリーDOI: 10.2210/pdb4er2/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000557
• 分子名称: ENDOTHIAPEPSIN, PEPSTATIN, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: acid proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Cryphonectria parasitica (chestnut blight fungus); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34787.94

構造登録者

Bailey, D.,Veerapandian, B.,Cooper, J.B.,Blundell, T.L. (登録日: 1990-10-20, 公開日: 1991-01-15, 最終更新日: 2024-10-30)

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 Å)