2okn

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{{STRUCTURE_2okn| PDB=2okn | SCENE= }}
 
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===Crystal Strcture of Human Prolidase===
 
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==Disease==
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==Crystal Strcture of Human Prolidase==
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[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[http://omim.org/entry/170100 170100]]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref><ref>PMID:8198124</ref><ref>PMID:8900231</ref><ref>PMID:12384772</ref>
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<StructureSection load='2okn' size='340' side='right'caption='[[2okn]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[2okn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OKN FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PI:HYDROGENPHOSPHATE+ION'>PI</scene></td></tr>
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==About this Structure==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2okn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2okn OCA], [https://pdbe.org/2okn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2okn RCSB], [https://www.ebi.ac.uk/pdbsum/2okn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2okn ProSAT]</span></td></tr>
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[[2okn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKN OCA].
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</table>
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== Disease ==
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==Reference==
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[https://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[https://omim.org/entry/170100 170100]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>
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<references group="xtra"/><references/>
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== Function ==
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[https://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/2okn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2okn ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Xaa-Pro dipeptidase]]
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[[Category: Large Structures]]
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[[Category: Behlke, J.]]
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[[Category: Behlke J]]
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[[Category: Buessow, K.]]
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[[Category: Buessow K]]
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[[Category: Goetz, F.]]
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[[Category: Goetz F]]
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[[Category: Heinemann, U.]]
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[[Category: Heinemann U]]
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[[Category: Mueller, U.]]
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[[Category: Mueller U]]
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[[Category: Niesen, F H.]]
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[[Category: Niesen FH]]
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[[Category: PSF, Protein Structure Factory.]]
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[[Category: Roske Y]]
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[[Category: Roske, Y.]]
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[[Category: Collagen degradation]]
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[[Category: Dipeptidase]]
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[[Category: Disease mutation]]
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[[Category: Enzyme]]
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[[Category: Hydrolase]]
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[[Category: Manganese]]
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[[Category: Metal-binding]]
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[[Category: Metalloaminopeptidase]]
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[[Category: Metallocarboxypeptidase]]
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[[Category: Metalloprotease]]
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[[Category: Pepd gene]]
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[[Category: Peptidase d]]
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[[Category: Phosphorylation]]
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[[Category: Protease]]
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[[Category: Protein structure factory]]
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[[Category: Psf]]
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[[Category: Structural genomic]]
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[[Category: Xaa-pro dipeptidase]]
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Current revision

Crystal Strcture of Human Prolidase

PDB ID 2okn

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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