1er8

THE ACTIVE SITE OF ASPARTIC PROTEINASES

spinqualitylabelsall models 1er8, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1er8 is a 2 chain structure with sequence from Cryphonectria parasitica and Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: DHI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARP_CRYPA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The active site of aspartic proteinases.,Pearl L, Blundell T FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

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