1itq | pdb_00001itq

HUMAN RENAL DIPEPTIDASE

spinqualitylabelsall models 1itq, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1itq is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, ZN Related: 1itu Activity: Membrane dipeptidase, with EC number 3.4.13.19 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DPEP1_HUMAN] Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity. 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 Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease. Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis.,Nitanai Y, Satow Y, Adachi H, Tsujimoto M J Mol Biol. 2002 Aug 9;321(2):177-84. PMID:12144777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Metalloproteases

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