2xmc - Revision history

OCA at 10:34, 20 December 2023

OCA — Wed, 20 Dec 2023 10:34:23 GMT

←Older revision		Revision as of 10:34, 20 December 2023
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	<StructureSection load='2xmc' size='340' side='right'caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2xmc' size='340' side='right'caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XMC FirstGlance]. <br>
-	</td></tr><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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene~~>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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]] 2.4Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</div></td></tr>	+	<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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cholinesterase Cholinesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.8 3.1.1.8] </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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [https://pdbe.org/2xmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [https://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [https://pdbe.org/2xmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [https://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[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.	+	[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 ==
-	[[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>	+	[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 ==
Line 29:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cholinesterase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Carletti, E]]	+	[[Category: Carletti E]]
-	[[Category: Lockridge, O]]	+	[[Category: Lockridge O]]
-	[[Category: Masson, P]]	+	[[Category: Masson P]]
-	[[Category: Nachon, F]]	+	[[Category: Nachon F]]
-	[[Category: Nicolet, Y]]	+	[[Category: Nicolet Y]]
-	[[Category: Schopfer~~, L M~~]]	+	[[Category: Schopfer LM]]
-	[[Category: Wandhammer, M]]	+	[[Category: Wandhammer M]]
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 05:24, 10 August 2022

OCA — Wed, 10 Aug 2022 05:24:31 GMT

OCA at 08:01, 4 November 2020

OCA — Wed, 04 Nov 2020 08:01:46 GMT

←Older revision		Revision as of 08:01, 4 November 2020
Line 1:		Line 1:

	==G117H mutant of human butyrylcholinesterase in complex with fluoride anion==		==G117H mutant of human butyrylcholinesterase in complex with fluoride anion==
-	<StructureSection load='2xmc' size='340' side='right' caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='2xmc' size='340' side='right'caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2XMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XMC FirstGlance]. <br>
-	</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=F:FLUORIDE+ION'>F~~</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC~~</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>	+	</td></tr><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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>
	<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>		<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>
-	<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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [http://pdbe.org/2xmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [http://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [http://pdbe.org/2xmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [http://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 24:		Line 24:

	==See Also==		==See Also==
-	*[[Butyrylcholinesterase\|Butyrylcholinesterase]]	+	*[[Butyrylcholinesterase 3D structures\|Butyrylcholinesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 31:		Line 31:
	[[Category: Cholinesterase]]		[[Category: Cholinesterase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Carletti, E]]		[[Category: Carletti, E]]
	[[Category: Lockridge, O]]		[[Category: Lockridge, O]]

OCA at 09:25, 3 October 2018

OCA — Wed, 03 Oct 2018 09:25:38 GMT

←Older revision		Revision as of 09:25, 3 October 2018
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XMC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XMC FirstGlance]. <br>
-	</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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX~~</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC~~</scene></td></tr>	+	</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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>
	<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>		<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>

OCA at 20:52, 11 August 2016

OCA — Thu, 11 Aug 2016 20:52:04 GMT

←Older revision		Revision as of 20:52, 11 August 2016
Line 1:		Line 1:
		+
	==G117H mutant of human butyrylcholinesterase in complex with fluoride anion==		==G117H mutant of human butyrylcholinesterase in complex with fluoride anion==
	<StructureSection load='2xmc' size='340' side='right' caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2xmc' size='340' side='right' caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>
	<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>		<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>
-	<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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [http://www.ebi.ac.uk/pdbsum/2xmc 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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [http://pdbe.org/2xmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [http://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 2xmc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 08:19, 14 January 2015

OCA — Wed, 14 Jan 2015 08:19:53 GMT

←Older revision		Revision as of 08:19, 14 January 2015
Line 1:		Line 1:
-	==G117H ~~MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION~~==	+	==G117H mutant of human butyrylcholinesterase in complex with fluoride anion==
	<StructureSection load='2xmc' size='340' side='right' caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2xmc' size='340' side='right' caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xmc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XMC FirstGlance]. <br>
	</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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>		</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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Cholinesterase]]		[[Category: Cholinesterase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Carletti, E]]		[[Category: Carletti, E]]
	[[Category: Lockridge, O]]		[[Category: Lockridge, O]]

OCA at 12:09, 18 December 2014

OCA — Thu, 18 Dec 2014 12:09:23 GMT

←Older revision		Revision as of 12:09, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2xmc\| PDB=2xmc \| SCENE= }}~~	+	==G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION==
-	===G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION===	+	<StructureSection load='2xmc' size='340' side='right' caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21091433}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2xmc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XMC FirstGlance]. <br>
-	==Disease==	+	</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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>
		+	<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>
		+	<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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [http://www.ebi.ac.uk/pdbsum/2xmc PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[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.		[[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.
		+	== Function ==
		+	[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Organophosphylates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase, by phosphylation of the catalytic serine. Engineering of human butyrylcholinesterase by substitution of histidine for glycine at position 117 led to the creation of OP hydrolase activity. But the lack of structural information and poor understanding of the hydrolytic mechanism of G117H has hampered further improvements in the catalytic activity. We solved the crystallographic structure of the G117H mutant with a variety of ligands in the active site. A sulfate anion bound to the active site suggested the positioning for an OP prior to phosphylation. A fluoride anion was found in the active site when NaF was added to the crystallization buffer. In the fluoride complex, the imidazole ring from His117 was substantially shifted adopting a relaxed conformation most likely close to that of the unliganded mutant enzyme. Additional X-ray structures were obtained from the transient covalent adducts formed upon reaction of G117H with the OPs echothiophate and VX. The position of His117 shifted in response to the introduction of these adducts, overlaying the phosphylserine. These structural data suggest that the dephosphylation mechanism involves either a substantial conformational change of His117 or an adjacent nucleophilic substitution by water.

-	~~==Function==~~	+	X-ray crystallographic snapshots of reaction intermediates in the G117H mutant of human butyrylcholinesterase, a nerve agent target engineered into a catalytic bioscavenger.,Nachon F, Carletti E, Wandhammer M, Nicolet Y, Schopfer LM, Masson P, Lockridge O Biochem J. 2010 Nov 19. PMID:21091433<ref>PMID:21091433</ref>
-	~~[[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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[2xmc]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Butyrylcholinesterase\|Butyrylcholinesterase]]		*[[Butyrylcholinesterase\|Butyrylcholinesterase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021091433</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Cholinesterase]]		[[Category: Cholinesterase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Carletti, E.]]	+	[[Category: Carletti, E]]
-	[[Category: Lockridge, O.]]	+	[[Category: Lockridge, O]]
-	[[Category: Masson, P.]]	+	[[Category: Masson, P]]
-	[[Category: Nachon, F.]]	+	[[Category: Nachon, F]]
-	[[Category: Nicolet, Y.]]	+	[[Category: Nicolet, Y]]
-	[[Category: Schopfer, L M.]]	+	[[Category: Schopfer, L M]]
-	[[Category: Wandhammer, M.]]	+	[[Category: Wandhammer, M]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 06:47, 25 March 2013

OCA — Mon, 25 Mar 2013 06:47:27 GMT

←Older revision		Revision as of 06:47, 25 March 2013
Line 1:		Line 1:
-	[[Image:2xmc.png\|left\|200px]]
-
	{{STRUCTURE_2xmc\| PDB=2xmc \| SCENE= }}		{{STRUCTURE_2xmc\| PDB=2xmc \| SCENE= }}
-
	===G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION===		===G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION===
		+	{{ABSTRACT_PUBMED_21091433}}

-	~~{{ABSTRACT_PUBMED_21091433}}~~	+	==Disease==
		+	[[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.
		+
		+	==Function==
		+	[[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>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021091433</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021091433</ref><references group="xtra"/><references/>
	[[Category: Cholinesterase]]		[[Category: Cholinesterase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 22:27, 20 October 2012

OCA — Sat, 20 Oct 2012 22:27:26 GMT

←Older revision		Revision as of 22:27, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2xmc]] is a 1 chain structure ~~of [[Butyrylcholinesterase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA].	+	[[2xmc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA].

	==See Also==		==See Also==

OCA at 16:21, 27 July 2012

OCA — Fri, 27 Jul 2012 16:21:16 GMT

←Older revision		Revision as of 16:21, 27 July 2012
Line 1:		Line 1:
	[[Image:2xmc.png\|left\|200px]]		[[Image:2xmc.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2xmc", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2xmc\| PDB=2xmc \| SCENE= }}		{{STRUCTURE_2xmc\| PDB=2xmc \| SCENE= }}

	===G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION===		===G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH FLUORIDE ANION===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21091433}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21091433 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_21091433}}		{{ABSTRACT_PUBMED_21091433}}

Line 22:		Line 11:

	==See Also==		==See Also==
-	*[[Butyrylcholinesterase]]	+	*[[Butyrylcholinesterase\|Butyrylcholinesterase]]

	==Reference==		==Reference==

←Older revision		Revision as of 05:24, 10 August 2022
Line 3:		Line 3:
	<StructureSection load='2xmc' size='340' side='right'caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='2xmc' size='340' side='right'caption='[[2xmc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xmc]] is a 1 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=2XMC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2XMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XMC FirstGlance]. <br>
	</td></tr><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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>		</td></tr><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=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wsl\|2wsl]], [[2j4c\|2j4c]], [[2wik\|2wik]], [[1kcj\|1kcj]], [[1p0p\|1p0p]], [[1xlu\|1xlu]], [[2wij\|2wij]], [[1xlv\|1xlv]], [[1eho\|1eho]], [[1p0m\|1p0m]], [[1xlw\|1xlw]], [[1ehq\|1ehq]], [[1p0q\|1p0q]], [[2wid\|2wid]], [[2wil\|2wil]], [[2wif\|2wif]], [[1p0i\|1p0i]], [[2wig\|2wig]], [[2xmd\|2xmd]], [[2xmb\|2xmb]], [[2xmg\|2xmg]]</div></td></tr>
-	<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>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cholinesterase Cholinesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.8 3.1.1.8] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [~~http~~://pdbe.org/2xmc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</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=2xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmc OCA], [https://pdbe.org/2xmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xmc RCSB], [https://www.ebi.ac.uk/pdbsum/2xmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~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.	+	[[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 ==
-	[[~~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>	+	[[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 ==