3cpa
From Proteopedia
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|PDB= 3cpa |SIZE=350|CAPTION= <scene name='initialview01'>3cpa</scene>, resolution 2.0Å | |PDB= 3cpa |SIZE=350|CAPTION= <scene name='initialview01'>3cpa</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cpa OCA], [http://www.ebi.ac.uk/pdbsum/3cpa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3cpa RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lipscomb, W N.]] | [[Category: Lipscomb, W N.]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase (c-terminal peptidase)]] | [[Category: hydrolase (c-terminal peptidase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:32:41 2008'' |
Revision as of 02:32, 31 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Carboxypeptidase A, with EC number 3.4.17.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 05:32:41 2008
