1amh
UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)
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| , resolution 2.5Å | |||||||
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| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
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 Thu Mar 20 09:59:32 2008