2h7c: Difference between revisions

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==Crystal structure of human carboxylesterase in complex with Coenzyme A==
==Crystal structure of human carboxylesterase in complex with Coenzyme A==
<StructureSection load='2h7c' size='340' side='right' caption='[[2h7c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2h7c' size='340' side='right'caption='[[2h7c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2h7c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H7C FirstGlance]. <br>
<table><tr><td colspan='2'>[[2h7c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H7C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mx1|1mx1]], [[1mx5|1mx5]], [[1mx9|1mx9]], [[1ya4|1ya4]], [[1ya8|1ya8]], [[1yah|1yah]], [[2dqy|2dqy]], [[2dqz|2dqz]], [[2dr0|2dr0]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></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=2h7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h7c OCA], [https://pdbe.org/2h7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h7c RCSB], [https://www.ebi.ac.uk/pdbsum/2h7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h7c ProSAT]</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=2h7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h7c OCA], [http://pdbe.org/2h7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h7c RCSB], [http://www.ebi.ac.uk/pdbsum/2h7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h7c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EST1_HUMAN EST1_HUMAN]] Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate.<ref>PMID:7980644</ref> <ref>PMID:9169443</ref>
[https://www.uniprot.org/uniprot/EST1_HUMAN EST1_HUMAN] Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate.<ref>PMID:7980644</ref> <ref>PMID:9169443</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Carboxylesterase|Carboxylesterase]]
*[[Carboxylesterase|Carboxylesterase]]
*[[Journal:Acta Cryst F:S1744309112003326|Journal:Acta Cryst F:S1744309112003326]]
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carboxylesterase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Bencharit, S]]
[[Category: Bencharit S]]
[[Category: Edwards, C C]]
[[Category: Edwards CC]]
[[Category: Howard-Williams, E L]]
[[Category: Howard-Williams EL]]
[[Category: Morton, C L]]
[[Category: Morton CL]]
[[Category: Potter, P M]]
[[Category: Potter PM]]
[[Category: Redinbo, M R]]
[[Category: Redinbo MR]]
[[Category: Cholesteryl esterase]]
[[Category: Enzyme]]
[[Category: Esterase]]
[[Category: Hydrolase]]

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