1amh

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Image:1amh.jpg

1amh, resolution 2.5Å

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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.

About this Structure

1AMH is a Single protein structure of sequence from Rattus rattus with as ligand. Active as Trypsin, with EC number 3.4.21.4 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

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

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