3ixl
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | |||
==Crystal structure of the Gly74Cys-Cys188Ser mutant of arylmalonate decarboxylase in the liganded form== | ==Crystal structure of the Gly74Cys-Cys188Ser mutant of arylmalonate decarboxylase in the liganded form== | ||
<StructureSection load='3ixl' size='340' side='right' caption='[[3ixl]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='3ixl' size='340' side='right' caption='[[3ixl]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ixl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3ixl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"alcaligenes_bronchicanis"_(ferry_1911)_haupt_1935 "alcaligenes bronchicanis" (ferry 1911) haupt 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IXL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IXL FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PAC:2-PHENYLACETIC+ACID'>PAC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PAC:2-PHENYLACETIC+ACID'>PAC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ixm|3ixm]], [[3dtv|3dtv]], [[3dg9|3dg9]], [[2vlb|2vlb]], [[2dgd|2dgd]], [[1zuw|1zuw]], [[2dx7|2dx7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ixm|3ixm]], [[3dtv|3dtv]], [[3dg9|3dg9]], [[2vlb|2vlb]], [[2dgd|2dgd]], [[1zuw|1zuw]], [[2dx7|2dx7]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arylmalonate_decarboxylase Arylmalonate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.76 4.1.1.76] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arylmalonate_decarboxylase Arylmalonate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.76 4.1.1.76] </span></td></tr> | ||
| - | <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=3ixl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ixl RCSB], [http://www.ebi.ac.uk/pdbsum/3ixl PDBsum]</span></td></tr> | + | <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=3ixl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixl OCA], [http://pdbe.org/3ixl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ixl RCSB], [http://www.ebi.ac.uk/pdbsum/3ixl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ixl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 17: | Line 18: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3ixl ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 27: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3ixl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 32: | Line 34: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arylmalonate decarboxylase]] | [[Category: Arylmalonate decarboxylase]] | ||
| - | [[Category: Bordetella bronchiseptica]] | ||
[[Category: Nakasako, M]] | [[Category: Nakasako, M]] | ||
[[Category: Obata, R]] | [[Category: Obata, R]] | ||
Revision as of 09:38, 5 August 2016
Crystal structure of the Gly74Cys-Cys188Ser mutant of arylmalonate decarboxylase in the liganded form
| |||||||||||
