1ffq: Difference between revisions

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OCA

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-[[Image:1ffq.gif|left|200px]]<br /><applet load="1ffq" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ffq, resolution 1.9&Aring;" />
-'''CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN==
-The purification scheme of chitinase A (ChiA) from S. marcescens has been, extensively revised. The pure enzyme crystallizes readily under new, crystallization conditions. The ChiA crystal structure has been refined to, 1.55 A resolution and the crystal structure of ChiA co-crystallized with, the inhibitor allosamidin has been refined to 1.9 A resolution., Allosamidin is located in the deep active-site tunnel of ChiA and, interacts with three important residues: Glu315, the proton donor of the, catalysis, Asp313, which adopts two conformations in the native structure, but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which, lies opposite Glu315 in the active-site tunnel.
+<StructureSection load='1ffq' size='340' side='right'caption='[[1ffq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ffq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMI:ALLOSAMIZOLINE'>AMI</scene>, <scene name='pdbligand=NAA:N-ACETYL-D-ALLOSAMINE'>NAA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffq OCA], [https://pdbe.org/1ffq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffq RCSB], [https://www.ebi.ac.uk/pdbsum/1ffq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHIA_SERMA CHIA_SERMA]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/1ffq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ffq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.
-==About this Structure==
+De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.,Papanikolau Y, Tavlas G, Vorgias CE, Petratos K Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):400-3. Epub 2003, Jan 23. PMID:12554965<ref>PMID:12554965</ref>
-FFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with AMI as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFQ OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin., Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):400-3. Epub 2003, Jan 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12554965 12554965]
+</div>
-[[Category: Chitinase]]
+<div class="pdbe-citations 1ffq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Chitinase 3D structures|Chitinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Serratia marcescens]]
-[[Category: Single protein]]
+[[Category: Papanikolau Y]]
-[[Category: Papanikolau, Y.]]
+[[Category: Petratos K]]
-[[Category: Petratos, K.]]
+[[Category: Tavlas G]]
-[[Category: Tavlas, G.]]
+[[Category: Vorgias CE]]
-[[Category: Vorgias, C.E.]]
-[[Category: AMI]]
-[[Category: enzyme-inhibitor complex]]
-[[Category: glycosyl hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:53:21 2007''