1cbx

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[[Image:1cbx.gif|left|200px]]
[[Image:1cbx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1cbx |SIZE=350|CAPTION= <scene name='initialview01'>1cbx</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1cbx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BZS:L-BENZYLSUCCINIC+ACID'>BZS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1cbx| PDB=1cbx | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbx OCA], [http://www.ebi.ac.uk/pdbsum/1cbx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cbx RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION'''
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION'''
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[[Category: Mangani, S.]]
[[Category: Mangani, S.]]
[[Category: Orioli, P.]]
[[Category: Orioli, P.]]
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[[Category: hydrolase(c-terminal peptidase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:33:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:40 2008''
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Revision as of 09:33, 2 May 2008

Image:1cbx.gif

Template:STRUCTURE 1cbx

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION


Overview

The X-ray crystal structure of the carboxypeptidase A-L-benzylsuccinate complex has been refined at 2.0 A resolution to a final R-factor of 0.166. One molecule of the inhibitor binds to the enzyme active site. The terminal carboxylate forms a salt link with the guanidinium group of Arg145 and hydrogen bonds with Tyr248 and Asn144. The second carboxylate group binds to the zinc ion in an asymmetric bidentate fashion replacing the water molecule of the native structure. The zinc ion moves 0.5 A from its position in the native structure to accommodate the inhibitor binding. The overall stereochemistry around the zinc can be considered a distorted tetrahedron, although six atoms of the co-ordinated groups lie within 3.0 A from the zinc ion. The key for the strong inhibitory properties of L-benzylsuccinate can be found in its ability both to co-ordinate the zinc and to form a short carboxyl-carboxylate-type hydrogen bond (2.5 A) with Glu270.

About this Structure

1CBX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution., Mangani S, Carloni P, Orioli P, J Mol Biol. 1992 Jan 20;223(2):573-8. PMID:1738164 Page seeded by OCA on Fri May 2 12:33:42 2008

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