1au9: Difference between revisions

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[[Image:1au9.gif|left|200px]]<br /><applet load="1au9" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1au9.gif|left|200px]]
caption="1au9, resolution 1.80&Aring;" />
 
'''SUBTILISIN BPN' MUTANT 8324 IN CITRATE'''<br />
{{Structure
|PDB= 1au9 |SIZE=350|CAPTION= <scene name='initialview01'>1au9</scene>, resolution 1.80&Aring;
|SITE= <scene name='pdbsite=169:Mutation+From+GLY+To+ALA+At+Residue+169'>169</scene>, <scene name='pdbsite=206:Mutation+From+GLN+To+CYS+At+Residue+206.+An+Unknown+Thio+...'>206</scene>, <scene name='pdbsite=217:Mutation+From+TYR+To+LYS+At+Residue+217'>217</scene>, <scene name='pdbsite=218:Mutation+From+ASN+To+SER+At+Residue+218'>218</scene>, <scene name='pdbsite=C22:Mutation+From+THR+To+CYS+At+Residue+22.+CYS+22+Forms+A+D+...'>C22</scene>, <scene name='pdbsite=C87:Mutation+From+SER+To+CYS+At+Residue+87.+CYS+87+Forms+A+D+...'>C87</scene>, <scene name='pdbsite=CA1:High+Affinity+Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Low+Affinity+Ca+Binding+Site'>CA2</scene> and <scene name='pdbsite=F50:Mutation+From+MET+To+PHE+At+Residue+50'>F50</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene> and <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]
|GENE=
}}
 
'''SUBTILISIN BPN' MUTANT 8324 IN CITRATE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1AU9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=UNX:'>UNX</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Known structural/functional Sites: <scene name='pdbsite=169:Mutation+From+GLY+To+ALA+At+Residue+169'>169</scene>, <scene name='pdbsite=206:Mutation+From+GLN+To+CYS+At+Residue+206.+An+Unknown+Thio+...'>206</scene>, <scene name='pdbsite=217:Mutation+From+TYR+To+LYS+At+Residue+217'>217</scene>, <scene name='pdbsite=218:Mutation+From+ASN+To+SER+At+Residue+218'>218</scene>, <scene name='pdbsite=C22:Mutation+From+THR+To+CYS+At+Residue+22.+CYS+22+Forms+A+D+...'>C22</scene>, <scene name='pdbsite=C87:Mutation+From+SER+To+CYS+At+Residue+87.+CYS+87+Forms+A+D+...'>C87</scene>, <scene name='pdbsite=CA1:High+Affinity+Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Low+Affinity+Ca+Binding+Site'>CA2</scene> and <scene name='pdbsite=F50:Mutation+From+MET+To+PHE+At+Residue+50'>F50</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU9 OCA].  
1AU9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU9 OCA].  


==Reference==
==Reference==
Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding., Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN, Biochemistry. 1989 Sep 5;28(18):7205-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2684274 2684274]
Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding., Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN, Biochemistry. 1989 Sep 5;28(18):7205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2684274 2684274]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: serine protease]]
[[Category: serine protease]]


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