1ept

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[[Image:1ept.gif|left|200px]]
[[Image:1ept.gif|left|200px]]
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{{Structure
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|PDB= 1ept |SIZE=350|CAPTION= <scene name='initialview01'>1ept</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1ept", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</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/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span>
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{{STRUCTURE_1ept| PDB=1ept | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ept FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ept OCA], [http://www.ebi.ac.uk/pdbsum/1ept PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ept RCSB]</span>
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'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN'''
'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN'''
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[[Category: Tang, Y.]]
[[Category: Tang, Y.]]
[[Category: Wang, Z.]]
[[Category: Wang, Z.]]
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[[Category: hydrolase (serine protease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:23:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:22 2008''
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Revision as of 12:23, 2 May 2008

Image:1ept.gif

Template:STRUCTURE 1ept

REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN


Overview

Porcine epsilon-trypsin is a three-chain inactivated trypsin from the limited autolysis of porcine beta-trypsin. It is cleaved at positions Lys60-Ser61 and Lys145-Ser146. The crystal structure has been determined by using the molecular replacement method, and refined at 1.8 A resolution. The R-value of final model is 0.184. Comparison with the electron density map of porcine beta-trypsin (PTRY) in complex (BBIT), and with that of native bovine beta-trypsin (HTNA), revealed no obvious changes except at the autolysis positions, and no changes at the active center were observed. The autolysis at positions Lys60-Ser61 and Lys145-Ser146 does not affect the conformation of His-57 in the active center and therefore cannot explain for a loss in porcine epsilon-trypsin activity.

About this Structure

1EPT is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin., Huang Q, Wang Z, Li Y, Liu S, Tang Y, Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:7947985 Page seeded by OCA on Fri May 2 15:23:07 2008

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