1oex

Atomic Resolution Structure of Endothiapepsin in Complex with a Hydroxyethylene Transition State Analogue Inhibitor H261

spinqualitylabelsall models 1oex, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1oex is a 2 chain structure with sequence from Cryphonectria parasitica and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: BOC, GOL, LOV, SO4, SUI 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 X-ray structures of native endothiapepsin and a complex with a hydroxyethylene transition state analog inhibitor (H261) have been determined at atomic resolution. Unrestrained refinement of the carboxyl groups of the enzyme by using the atomic resolution data indicates that both catalytic aspartates in the native enzyme share a single negative charge equally; that is, in the crystal, one half of the active sites have Asp 32 ionized and the other half have Asp 215 ionized. The electron density map of the native enzyme refined at 0.9 A resolution demonstrates that there is a short peptide (probably Ser-Thr) bound noncovalently in the active site cleft. The N-terminal nitrogen of the dipeptide interacts with the aspartate diad of the enzyme by hydrogen bonds involving the carboxyl of Asp 215 and the catalytic water molecule. This is consistent with classical findings that the aspartic proteinases can be inhibited weakly by short peptides and that these enzymes can catalyze transpeptidation reactions. The dipeptide may originate from autolysis of the N-terminal Ser-Thr sequence of the enzyme during crystallization. Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.,Erskine PT, Coates L, Mall S, Gill RS, Wood SP, Myles DA, Cooper JB Protein Sci. 2003 Aug;12(8):1741-9. PMID:12876323 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

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