5cpa

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[[Image:5cpa.gif|left|200px]]
[[Image:5cpa.gif|left|200px]]
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{{Structure
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|PDB= 5cpa |SIZE=350|CAPTION= <scene name='initialview01'>5cpa</scene>, resolution 1.54&Aring;
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The line below this paragraph, containing "STRUCTURE_5cpa", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <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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{{STRUCTURE_5cpa| PDB=5cpa | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cpa OCA], [http://www.ebi.ac.uk/pdbsum/5cpa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5cpa RCSB]</span>
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'''REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.'''
'''REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lipscomb, W N.]]
[[Category: Lipscomb, W N.]]
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[[Category: hydrolase (c-terminal peptidase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:32:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:41:06 2008''
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Revision as of 19:32, 4 May 2008

Template:STRUCTURE 5cpa

REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.


Overview

The crystal structure of bovine carboxypeptidase A (Cox) has been refined at 1.54 A resolution using the restrained least-squares algorithm of Hendrickson & Konnert (1981). The crystallographic R factor (formula; see text) for structure factors calculated from the final model is 0.190. Bond lengths and bond angles in the carboxypeptidase A model have root-mean-square deviations from ideal values of 0.025 A and 3.6 degrees, respectively. Four examples of a reverse turn like structure (the "Asx" turn) requiring an aspartic acid or asparagine residue are observed in this structure. The Asx turn has the same number of atoms as a reverse turn, but only one peptide bond, and the hydrogen bond that closes the turn is between the Asx side-chain CO group and a main-chain NH group. The distributions of CO-N and NH-O hydrogen bond angles in the alpha-helices and beta-sheet structures of carboxypeptidase A are centered about 156 degrees. A total of 192 water molecules per molecule of enzyme are included in the final model. Unlike the hydrogen bonding geometry observed in the secondary structure of the enzyme, the CO-O(wat) hydrogen bond angle is distributed about 131 degrees, indicating the role of the lone pair electrons of the carbonyl oxygen in the hydrogen bond interaction. Twenty four solvent molecules are observed buried within the protein. Several of these waters are organized into hydrogen-bonded chains containing up to five waters. The average temperature factor for atoms in carboxypeptidase A is 8 A2, and varies from 5 A2 in the center of the protein, to over 30 A2 at the surface.

About this Structure

5CPA is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Refined crystal structure of carboxypeptidase A at 1.54 A resolution., Rees DC, Lewis M, Lipscomb WN, J Mol Biol. 1983 Aug 5;168(2):367-87. PMID:6887246 Page seeded by OCA on Sun May 4 22:32:58 2008

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