1flh: Difference between revisions

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{{STRUCTURE_1flh|  PDB=1flh  |  SCENE=  }}  
{{STRUCTURE_1flh|  PDB=1flh  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION'''
===CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11679720}}


==About this Structure==
==About this Structure==
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[[Category: Acid proteinase]]
[[Category: Acid proteinase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 03:26, 1 July 2008

File:1flh.png

Template:STRUCTURE 1flh

CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTIONCRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION

Template:ABSTRACT PUBMED 11679720

About this StructureAbout this Structure

1FLH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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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