2er6

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[[Image:2er6.jpg|left|200px]]
[[Image:2er6.jpg|left|200px]]
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{{Structure
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|PDB= 2er6 |SIZE=350|CAPTION= <scene name='initialview01'>2er6</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_2er6", creates the "Structure Box" on the page.
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|SITE=
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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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] </span>
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{{STRUCTURE_2er6| PDB=2er6 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2er6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2er6 OCA], [http://www.ebi.ac.uk/pdbsum/2er6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2er6 RCSB]</span>
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'''THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.'''
'''THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.'''
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[[Category: Foundling, S I.]]
[[Category: Foundling, S I.]]
[[Category: Szelke, M.]]
[[Category: Szelke, M.]]
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[[Category: hydrolase (acid proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:01:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:52:41 2008''
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Revision as of 00:01, 4 May 2008

Image:2er6.jpg

Template:STRUCTURE 2er6

THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.


Overview

The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X-ray diffraction at 0.20-nm resolution and refined to an agreement factor of 0.20. The inhibitor: Pro Thr Glu Phe-R-Phe Arg Glu (R = -CH2NH-) is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in place of the scissile bond, a reduced peptide group which is resistant to hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in an extended conformation with the reduced bond close to the essential aspartate side-chains of the enzyme. The hydrogen bonds and hydrophobic interactions between the enzyme and the inhibitor do not induce large conformational changes.

About this Structure

2ER6 is a Single protein structure of sequence from Cryphonectria parasitica. Full crystallographic information is available from OCA.

Reference

The structure of a synthetic pepsin inhibitor complexed with endothiapepsin., Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M, Eur J Biochem. 1987 Nov 16;169(1):215-21. PMID:3119339 Page seeded by OCA on Sun May 4 03:01:35 2008

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