3kvz

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==Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase FlK - wild type FlK in complex with FAcCPan==
==Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase FlK - wild type FlK in complex with FAcCPan==
<StructureSection load='3kvz' size='340' side='right' caption='[[3kvz]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3kvz' size='340' side='right' caption='[[3kvz]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3kvz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KVZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3kvz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KVZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ENV:(2R)-N-{3-[(5-FLUORO-4-OXOPENTYL)AMINO]-3-OXOPROPYL}-2,4-DIHYDROXY-3,3-DIMETHYLBUTANAMIDE'>ENV</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ENV:(2R)-N-{3-[(5-FLUORO-4-OXOPENTYL)AMINO]-3-OXOPROPYL}-2,4-DIHYDROXY-3,3-DIMETHYLBUTANAMIDE'>ENV</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kuv|3kuv]], [[3kuw|3kuw]], [[3kv7|3kv7]], [[3kv8|3kv8]], [[3kvi|3kvi]], [[3kvu|3kvu]], [[3kw1|3kw1]], [[3kx7|3kx7]], [[3kx8|3kx8]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kuv|3kuv]], [[3kuw|3kuw]], [[3kv7|3kv7]], [[3kv8|3kv8]], [[3kvi|3kvi]], [[3kvu|3kvu]], [[3kw1|3kw1]], [[3kx7|3kx7]], [[3kx8|3kx8]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flK, fluoroacetyl-CoA thioesterase FlK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 Streptomyces cattleya])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flK, fluoroacetyl-CoA thioesterase FlK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</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=3kvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kvz RCSB], [http://www.ebi.ac.uk/pdbsum/3kvz 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=3kvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kvz OCA], [http://pdbe.org/3kvz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kvz RCSB], [http://www.ebi.ac.uk/pdbsum/3kvz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kvz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q1EMV2_STRCT Q1EMV2_STRCT]] Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Can not use acetyl-CoA as substrate.<ref>PMID:16720268</ref> <ref>PMID:20836570</ref>
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[[http://www.uniprot.org/uniprot/FLK_STRCT FLK_STRCT]] Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Can not use acetyl-CoA as substrate.<ref>PMID:16720268</ref> <ref>PMID:20836570</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3kvz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3kvz" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Streptomyces cattleya]]
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[[Category: Streptomyces cattleya kahan et al. 1979]]
[[Category: Blundell, T L]]
[[Category: Blundell, T L]]
[[Category: Chirgadze, D Y]]
[[Category: Chirgadze, D Y]]

Revision as of 21:05, 4 August 2016

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase FlK - wild type FlK in complex with FAcCPan

3kvz, resolution 2.10Å

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