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3cyv

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<StructureSection load='3cyv' size='340' side='right' caption='[[3cyv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3cyv' size='340' side='right' caption='[[3cyv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3cyv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CYV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3cyv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CYV FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">urod ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 Shigella flexneri])</td></tr>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">urod ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uroporphyrinogen_decarboxylase Uroporphyrinogen decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.37 4.1.1.37] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uroporphyrinogen_decarboxylase Uroporphyrinogen decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.37 4.1.1.37] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cyv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cyv RCSB], [http://www.ebi.ac.uk/pdbsum/3cyv PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cyv OCA], [http://pdbe.org/3cyv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cyv RCSB], [http://www.ebi.ac.uk/pdbsum/3cyv PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=3cyv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Shigella flexneri]]
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[[Category: Shigella paradysenteriae weldin 1927]]
[[Category: Uroporphyrinogen decarboxylase]]
[[Category: Uroporphyrinogen decarboxylase]]
[[Category: Bi, R]]
[[Category: Bi, R]]

Revision as of 10:42, 7 February 2016

Crystal structure of uroporphyrinogen decarboxylase from Shigella flexineri: new insights into its catalytic mechanism

3cyv, resolution 2.80Å

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