4bd0 | pdb_00004bd0

X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)

spinqualitylabelsall models 4bd0, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bd0 is a 1 chain structure with sequence from Escherichia coli BL21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.207Å Ligands: BZB, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BLT1_ECOLX Has strong cefotaxime-hydrolyzing activity. Publication Abstract from PubMed The mechanism by which class A beta-lactamase enzymes form an acyl-enzyme intermediate has been the emphasis of several studies. Here, we report on the use of neutron and high resolution X-ray diffraction to help elucidate the identity of the catalytic base in the acylation part of the mechanism. Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 beta-lactamase for the acylation reaction.,Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L J Biol Chem. 2012 Dec 18. PMID:23255594 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

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