1flh
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(New page: 200px<br /> <applet load="1flh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1flh, resolution 2.45Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:48, 12 November 2007
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CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION
Overview
The molecular structure of human uropepsin, an aspartic proteinase from, the urine produced in the form of pepsinogen A in the gastric mucosa, has, been determined by molecular replacement using human pepsin as the search, model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell, parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement, led to an R factor of 0.161 at 2.45 A resolution. The positions of 2437, non-H protein atoms in 326 residues have been determined and the model, contains 143 water molecules. The structure is bilobal, consisting of two, predominantly beta-sheet lobes which, as observed in other aspartic, proteinases, are related by a pseudo-twofold axis. A model of the, uropepsin-pepstatin complex has been constructed based on the, high-resolution crystal structure of pepsin complexed with pepstatin.
About this Structure
1FLH is a Single protein structure of sequence from Homo sapiens. Active as Pepsin A, with EC number 3.4.23.1 Full crystallographic information is available from OCA.
Reference
Structure of human uropepsin at 2.45 A resolution., Canduri F, Teodoro LG, Fadel V, Lorenzi CC, Hial V, Gomes RA, Neto JR, de Azevedo WF Jr, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1560-70. Epub 2001, Oct 25. PMID:11679720
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