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'''Unreleased structure'''


The entry 6qsc is ON HOLD  until Feb 20 2021
==Crystal Structure of Arg470His mutant of Human Prolidase with Mn ions and GlyPro ligand==
 
<StructureSection load='6qsc' size='340' side='right'caption='[[6qsc]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
Authors: Wilk, P., Wator, E., Weiss, M.S.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6qsc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QSC FirstGlance]. <br>
Description: Crystal Structure of Arg470His mutant of Human Prolidase with Mn ions and GlyPro ligand
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MH2:MANGANESE+ION,+1+HYDROXYL+COORDINATED'>MH2</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5m4g|5m4g]], [[5m4j|5m4j]], [[5mbz|5mbz]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qsc OCA], [http://pdbe.org/6qsc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qsc RCSB], [http://www.ebi.ac.uk/pdbsum/6qsc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qsc ProSAT]</span></td></tr>
</table>
== Disease ==
[[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> 
== Function ==
[[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.
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xaa-Pro dipeptidase]]
[[Category: Wator, E]]
[[Category: Weiss, M S]]
[[Category: Wilk, P]]
[[Category: Wilk, P]]
[[Category: Wator, E]]
[[Category: Dipeptidase]]
[[Category: Weiss, M.S]]
[[Category: Hydrolase]]
[[Category: Metal binding]]
[[Category: Mutation]]
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