1amh: Difference between revisions

Revision as of 17:09, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1amh.png

Template:STRUCTURE 1amh

UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)

Template:ABSTRACT PUBMED 7795518

About this StructureAbout this Structure

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

ReferenceReference

Structural basis of substrate specificity in the serine proteases., Perona JJ, Craik CS, Protein Sci. 1995 Mar;4(3):337-60. PMID:7795518

Page seeded by OCA on Mon Jun 30 17:09:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1amh|  PDB=1amh  |  SCENE=  }}
-'''UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)'''
+===UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)===
-==Overview==
+<!--
-Structure-based mutational analysis of serine protease specificity has produced a large database of information useful in addressing biological function and in establishing a basis for targeted design efforts. Critical issues examined include the function of water molecules in providing strength and specificity of binding, the extent to which binding subsites are interdependent, and the roles of polypeptide chain flexibility and distal structural elements in contributing to specificity profiles. The studies also provide a foundation for exploring why specificity modification can be either straightforward or complex, depending on the particular system.
+The line below this paragraph, {{ABSTRACT_PUBMED_7795518}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_7795518}}
 ==About this Structure==
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 [[Category: Serine protease]]
 [[Category: Substrate specificity hydrolase]]
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