1amh: Difference between revisions
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[[Image:1amh. | [[Image:1amh.jpg|left|200px]]<br /><applet load="1amh" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1amh" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1amh, resolution 2.5Å" /> | caption="1amh, resolution 2.5Å" /> | ||
'''UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)'''<br /> | '''UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1AMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] | 1AMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=CAA:Catalytic Site'>CAA</scene> and <scene name='pdbsite=CAB:Catalytic Site'>CAB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AMH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: substrate specificity hydrolase]] | [[Category: substrate specificity hydrolase]] | ||
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Revision as of 15:08, 18 December 2007
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UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)
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 with CA as ligand. Active as Trypsin, with EC number 3.4.21.4 Known structural/functional Sites: and . 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
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