3fx6: Difference between revisions
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==X-RAY crystallographic studies on the complex of carboxypeptidase A with the inhibitor using alpha-nitro ketone as the zinc-binding group== | ==X-RAY crystallographic studies on the complex of carboxypeptidase A with the inhibitor using alpha-nitro ketone as the zinc-binding group== | ||
<StructureSection load='3fx6' size='340' side='right' caption='[[3fx6]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='3fx6' size='340' side='right' caption='[[3fx6]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BPX:(2R)-4,4-DIHYDROXY-5-NITRO-2-(PHENYLMETHYL)PENTANOIC+ACID'>BPX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BPX:(2R)-4,4-DIHYDROXY-5-NITRO-2-(PHENYLMETHYL)PENTANOIC+ACID'>BPX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1] </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=3fx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fx6 OCA], [http://pdbe.org/3fx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3fx6 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=3fx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fx6 OCA], [http://pdbe.org/3fx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3fx6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fx6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3fx6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3fx6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Metalloprotease]] | [[Category: Metalloprotease]] | ||
[[Category: Polymorphism]] | |||
[[Category: Protease]] | [[Category: Protease]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
[[Category: Zinc]] | |||
[[Category: Zymogen]] | [[Category: Zymogen]] | ||
Revision as of 09:51, 1 November 2017
X-RAY crystallographic studies on the complex of carboxypeptidase A with the inhibitor using alpha-nitro ketone as the zinc-binding groupX-RAY crystallographic studies on the complex of carboxypeptidase A with the inhibitor using alpha-nitro ketone as the zinc-binding group
Structural highlights
Function[CBPA1_BOVIN] Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedZinc-binding groups (ZBGs) are exhaustively applied in the development of the new inhibitors against a wide variety of physiologically and pathologically important zinc proteases. Here the alpha-nitro ketone was presented as a new ZBG, which is a transition-state analog featured by the unique bifurcated hydrogen bonds at the active site of carboxypeptidase A based on the structural analysis. Introduction of a nitro group at the alpha-position of the ketone could provide more non-covalent interactions without loss of the abilities to form a tetrahedral transition-state analog. Characterization of alpha-nitromethyl ketone as a new zinc-binding group based on structural analysis of its complex with carboxypeptidase A.,Wang SF, Tian GR, Zhang WZ, Jin JY Bioorg Med Chem Lett. 2009 Sep 1;19(17):5009-11. Epub 2009 Jul 12. PMID:19646864[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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