1dpo

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[[Image:1dpo.gif|left|200px]]<br /><applet load="1dpo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dpo.gif|left|200px]]
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caption="1dpo, resolution 1.59&Aring;" />
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'''STRUCTURE OF RAT TRYPSIN'''<br />
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{{Structure
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|PDB= 1dpo |SIZE=350|CAPTION= <scene name='initialview01'>1dpo</scene>, resolution 1.59&Aring;
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|SITE= <scene name='pdbsite=CAT:Catalytic+Triad'>CAT</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4]
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|GENE=
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}}
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'''STRUCTURE OF RAT TRYPSIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BEN:'>BEN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic+Triad'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPO OCA].
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1DPO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPO OCA].
==Reference==
==Reference==
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1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures., Earnest T, Fauman E, Craik CS, Stroud R, Proteins. 1991;10(3):171-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1881877 1881877]
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1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures., Earnest T, Fauman E, Craik CS, Stroud R, Proteins. 1991;10(3):171-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1881877 1881877]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: multigene family]]
[[Category: multigene family]]
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[[Category: pancreas]]
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[[Category: pancrea]]
[[Category: serine protease]]
[[Category: serine protease]]
[[Category: signal]]
[[Category: signal]]
[[Category: zymogen]]
[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:17 2008''

Revision as of 08:42, 20 March 2008

Image:1dpo.gif


PDB ID 1dpo

Drag the structure with the mouse to rotate
, resolution 1.59Å
Sites:
Ligands: , and
Activity: Trypsin, with EC number 3.4.21.4
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF RAT TRYPSIN


Overview

The structure of a rat trypsin mutant [S195C] at a temperature of 120 K has been refined to a crystallographic R factor of 17.4% between 12.0 and 1.59 A and is compared with the structure of the D102N mutant at 295 K. A reduction in the unit cell dimensions in going from room temperature to low temperature is accompanied by a decrease in molecular surface area and radius of gyration. The overall structure remains similar to that at room temperature. The attainable resolution appears to be improved due to the decrease in the fall off of intensities with resolution [reduction of the temperature factor]. This decreases the uncertainty in the atomic positions and allows the localization of more protein atoms and solvent molecules in the low temperature map. The largest differences between the two models occur at residues with higher than average temperature factors. Several features can be localized in the solvent region of the 120 K map that are not seen in the 295 K map. These include several more water molecules as well as an interstitial sulfate ion and two interstitial benzamidine molecules.

About this Structure

1DPO is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.

Reference

1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures., Earnest T, Fauman E, Craik CS, Stroud R, Proteins. 1991;10(3):171-87. PMID:1881877

Page seeded by OCA on Thu Mar 20 10:42:17 2008

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