6eyf
From Proteopedia
(Difference between revisions)
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<StructureSection load='6eyf' size='340' side='right'caption='[[6eyf]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6eyf' size='340' side='right'caption='[[6eyf]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6eyf]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6eyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6eul 6eul]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EYF FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BY2:[3-[(1~{R})-1-(dimethylamino)ethyl]-4-oxidanyl-phenyl]+~{N}-ethyl-~{N}-methyl-carbamate'>BY2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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" id="ligandDat"><scene name='pdbligand=BXT:(2~{S})-2-azanyl-3-[ethyl(methyl)carbamoyl]oxy-propanoic+acid'>BXT</scene>, <scene name='pdbligand=BY2:[3-[(1~{R})-1-(dimethylamino)ethyl]-4-oxidanyl-phenyl]+~{N}-ethyl-~{N}-methyl-carbamate'>BY2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6eyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eyf OCA], [https://pdbe.org/6eyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eyf RCSB], [https://www.ebi.ac.uk/pdbsum/6eyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eyf ProSAT]</span></td></tr> | |
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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. |
== 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> |
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+ | ==See Also== | ||
+ | *[[Butyrylcholinesterase 3D structures|Butyrylcholinesterase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Brazzolotto | + | [[Category: Brazzolotto X]] |
- | [[Category: | + | [[Category: De la Mora E]] |
- | [[Category: | + | [[Category: Dighe S]] |
- | [[Category: Ross | + | [[Category: Ross B]] |
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Current revision
Butyrylcolinesterase expressed in CHO cells co-crystallised with a rivastigmine analogue
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