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3n2z
From Proteopedia
(Difference between revisions)
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<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=3n2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n2z RCSB], [http://www.ebi.ac.uk/pdbsum/3n2z PDBsum]</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=3n2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n2z RCSB], [http://www.ebi.ac.uk/pdbsum/3n2z PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PCP_HUMAN PCP_HUMAN]] Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 08:37, 24 December 2014
The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution
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