1s5u: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s5u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S5U FirstGlance]. <br> | <table><tr><td colspan='2'>[[1s5u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S5U FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YBGC, B0736, C0815, Z0904, ECS0771, SF0561, S0574 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YBGC, B0736, C0815, Z0904, ECS0771, SF0561, S0574 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s5u RCSB], [http://www.ebi.ac.uk/pdbsum/1s5u PDBsum], [http://www.topsan.org/Proteins/MCSG/1s5u TOPSAN]</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=1s5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s5u RCSB], [http://www.ebi.ac.uk/pdbsum/1s5u PDBsum], [http://www.topsan.org/Proteins/MCSG/1s5u TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/YBGC_ECOLI YBGC_ECOLI]] Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Edwards, A | [[Category: Edwards, A]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: Kim, Y | [[Category: Kim, Y]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Savchenko, A | [[Category: Savchenko, A]] | ||
[[Category: Skarina, T | [[Category: Skarina, T]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Hypothetical protein]] | [[Category: Hypothetical protein]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Thioesterase fold]] | [[Category: Thioesterase fold]] | ||
Revision as of 20:38, 24 December 2014
Crystal Structure of Hypothetical Protein EC709 from Escherichia coliCrystal Structure of Hypothetical Protein EC709 from Escherichia coli
Structural highlights
Function[YBGC_ECOLI] Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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