3dyb

proteinase K- digalacturonic acid complex

spinqualitylabelsall models 3dyb, resolution 1.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dyb is a 1 chain structure with sequence from Engyodontium album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AD0, CA, EPE Activity: Peptidase K, with EC number 3.4.21.64 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PRTK_TRIAL] Hydrolyzes keratin at aromatic and hydrophobic residues. 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 Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside the protein, two calcium ions, 379 water molecules, a molecule of DGA and a partially occupied HEPES molecule. The DGA molecule has one sugar moiety disposed exactly on a crystallographic twofold axis; the second ring was not observed. The DGA molecule is bound to two protein molecules across the twofold axis through hydrogen-bonding networks involving Ser150 and water molecules. One of the calcium-ion sites has not been reported previously. This study further illustrates the involvement of small molecules in the crystallization of macromolecules through their ability to form intermolecular lattice interactions. High-resolution structure of proteinase K cocrystallized with digalacturonic acid.,Larson SB, Day JS, Nguyen C, Cudney R, McPherson A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):192-8. Epub 2009 Feb 12. PMID:19255463 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteinase

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