6rua

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<StructureSection load='6rua' size='340' side='right'caption='[[6rua]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='6rua' size='340' side='right'caption='[[6rua]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6rua]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RUA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RUA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6rua]] is a 2 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=6RUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RUA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=KJT:diethyl-[6-[[2-[2-[2-[naphthalen-2-ylsulfonyl-[[(3~{R})-1-(phenylmethyl)piperidin-3-yl]methyl]amino]ethoxy]ethoxy]ethylamino]-oxidanyl-methyl]-7-oxidanylidene-1,3,4,4~{a},5,6,8,8~{a}-octahydronaphthalen-2-ylidene]azanium'>KJT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dyt|5dyt]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=KJT:diethyl-[6-[[2-[2-[2-[naphthalen-2-ylsulfonyl-[[(3~{R})-1-(phenylmethyl)piperidin-3-yl]methyl]amino]ethoxy]ethoxy]ethylamino]-oxidanyl-methyl]-7-oxidanylidene-1,3,4,4~{a},5,6,8,8~{a}-octahydronaphthalen-2-ylidene]azanium'>KJT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cholinesterase Cholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.8 3.1.1.8] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rua OCA], [https://pdbe.org/6rua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rua RCSB], [https://www.ebi.ac.uk/pdbsum/6rua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rua ProSAT]</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=6rua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rua OCA], [http://pdbe.org/6rua PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rua RCSB], [http://www.ebi.ac.uk/pdbsum/6rua PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rua ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN]] Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) [MIM:[http://omim.org/entry/177400 177400]]. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait.
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[https://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN] Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) [MIM:[https://omim.org/entry/177400 177400]. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN]] Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.<ref>PMID:19542320</ref> <ref>PMID:19452557</ref>
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[https://www.uniprot.org/uniprot/CHLE_HUMAN CHLE_HUMAN] Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.<ref>PMID:19542320</ref> <ref>PMID:19452557</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6rua" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6rua" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Butyrylcholinesterase 3D structures|Butyrylcholinesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cholinesterase]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brus, B]]
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[[Category: Brus B]]
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[[Category: Colletier, J P]]
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[[Category: Colletier JP]]
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[[Category: Coquelle, N]]
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[[Category: Coquelle N]]
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[[Category: Gobec, S]]
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[[Category: Gobec S]]
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[[Category: Knez, D]]
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[[Category: Knez D]]
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[[Category: Fluorescent probe]]
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[[Category: Human butyrylcholinesterase]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Insect cell]]
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[[Category: Sulfonamide]]
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Current revision

Structure of recombinant human butyrylcholinesterase in complex with a coumarin-based fluorescent probe linked to sulfonamide type inhibitor.

PDB ID 6rua

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