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3cpa

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[[Image:3cpa.jpg|left|200px]]<br /><applet load="3cpa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3cpa.jpg|left|200px]]
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caption="3cpa, resolution 2.0&Aring;" />
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'''X-RAY CRYSTALLOGRAPHIC INVESTIGATION OF SUBSTRATE BINDING TO CARBOXYPEPTIDASE A AT SUBZERO TEMPERATURE'''<br />
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{{Structure
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|PDB= 3cpa |SIZE=350|CAPTION= <scene name='initialview01'>3cpa</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''X-RAY CRYSTALLOGRAPHIC INVESTIGATION OF SUBSTRATE BINDING TO CARBOXYPEPTIDASE A AT SUBZERO TEMPERATURE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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3CPA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1CPA. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CPA OCA].
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3CPA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure supersedes the now removed PDB entry 1CPA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CPA OCA].
==Reference==
==Reference==
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X-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperature., Christianson DW, Lipscomb WN, Proc Natl Acad Sci U S A. 1986 Oct;83(20):7568-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3463986 3463986]
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X-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperature., Christianson DW, Lipscomb WN, Proc Natl Acad Sci U S A. 1986 Oct;83(20):7568-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3463986 3463986]
[[Category: Carboxypeptidase A]]
[[Category: Carboxypeptidase A]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase (c-terminal peptidase)]]
[[Category: hydrolase (c-terminal peptidase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:18 2008''

Revision as of 17:04, 20 March 2008


PDB ID 3cpa

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands:
Activity: Carboxypeptidase A, with EC number 3.4.17.1
Coordinates: save as pdb, mmCIF, xml



X-RAY CRYSTALLOGRAPHIC INVESTIGATION OF SUBSTRATE BINDING TO CARBOXYPEPTIDASE A AT SUBZERO TEMPERATURE


Overview

A high-resolution x-ray crystallographic investigation of the complex between carboxypeptidase A (CPA; peptidyl-L-amino-acid hydrolase, EC 3.4.17.1) and the slowly hydrolyzed substrate glycyl-L-tyrosine was done at -9 degrees C. Although this enzyme-substrate complex has been the subject of earlier crystallographic investigation, a higher resolution electron-density map of the complex with greater occupancy of the substrate was desired. All crystal chemistry (i.e., crystal soaking and x-ray data collection) was performed on a diffractometer-mounted flow cell, in which the crystal was immobilized. The x-ray data to 1.6-A resolution have yielded a well-resolved structure in which the zinc ion of the active site is five-coordinate: three enzyme residues (glutamate-72, histidine-69, and histidine-196) and the carbonyl oxygen and amino terminus of glycyl-L-tyrosine complete the coordination polyhedron of the metal. These results confirm that this substrate may be bound in a nonproductive manner, because the hydrolytically important zinc-bound water has been displaced and excluded from the active site. It is likely that all dipeptide substrates of carboxypeptidase A that carry an unprotected amino terminus are poor substrates because of such favorable bidentate coordination to the metal ion of the active site.

About this Structure

3CPA is a Single protein structure of sequence from [1]. This structure supersedes the now removed PDB entry 1CPA. Full crystallographic information is available from OCA.

Reference

X-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperature., Christianson DW, Lipscomb WN, Proc Natl Acad Sci U S A. 1986 Oct;83(20):7568-72. PMID:3463986

Page seeded by OCA on Thu Mar 20 19:04:18 2008

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