1jrt

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[[Image:1jrt.gif|left|200px]]
[[Image:1jrt.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1jrt |SIZE=350|CAPTION= <scene name='initialview01'>1jrt</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1jrt", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1jrt| PDB=1jrt | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrt OCA], [http://www.ebi.ac.uk/pdbsum/1jrt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jrt RCSB]</span>
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}}
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'''HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN'''
'''HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN'''
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[[Category: Harrison, R W.]]
[[Category: Harrison, R W.]]
[[Category: Kurinov, I V.]]
[[Category: Kurinov, I V.]]
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[[Category: digestion]]
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[[Category: Digestion]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: pancrea]]
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[[Category: Pancrea]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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[[Category: zymogen]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:47:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:02 2008''
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Revision as of 18:47, 2 May 2008

Image:1jrt.gif

Template:STRUCTURE 1jrt

HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN


Overview

Three-dimensional structures of trypsin with the reversible inhibitor leupeptin have been determined in two different crystal forms. The first structure was determined at 1.7 A resolution with R-factor = 17.7% in the trigonal crystal space group P3(1)21, with unit cell dimensions of a = b = 55.62 A, c = 110.51 A. The second structure was determined at a resolution of 1.8 A with R-factor = 17.5% in the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 63.69 A, b = 69.37 A, c = 63.01 A. The overall protein structure is very similar in both crystal forms, with RMS difference for main-chain atoms of 0.27 A. The leupeptin backbone forms four hydrogen bonds with trypsin and a fifth hydrogen bond interaction is mediated by a water molecule. The aldehyde carbonyl of leupeptin forms a covalent bond of 1.42 A length with side-chain oxygen of Ser-195 in the active site. The reaction of trypsin with leupeptin proceeds through the formation of stable tetrahedral complex in which the hemiacetal oxygen atom is pointing out of the oxyanion hole and forming a hydrogen bond with His-57.

About this Structure

1JRT is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Two crystal structures of the leupeptin-trypsin complex., Kurinov IV, Harrison RW, Protein Sci. 1996 Apr;5(4):752-8. PMID:8845765 Page seeded by OCA on Fri May 2 21:47:18 2008

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