6dxx: Difference between revisions

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'''Unreleased structure'''


The entry 6dxx is ON HOLD until Paper Publication
==Human N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of Triton X-100==
 
<StructureSection load='6dxx' size='340' side='right' caption='[[6dxx]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6dxx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DXX FirstGlance]. <br>
Description:  
</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene>, <scene name='pdbligand=TON:2-{2-[4-(1,1,3,3-TETRAMETHYLBUTYL)PHENOXY]ETHOXY}ETHANOL'>TON</scene>, <scene name='pdbligand=WTF:[2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone'>WTF</scene></td></tr>
[[Category: Unreleased Structures]]
<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=6dxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dxx OCA], [http://pdbe.org/6dxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dxx RCSB], [http://www.ebi.ac.uk/pdbsum/6dxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dxx ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NAAA_HUMAN NAAA_HUMAN]] Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine.<ref>PMID:15655246</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gebai, A]]
[[Category: Gorelik, A]]
[[Category: Illes, K]]
[[Category: Nagar, B]]
[[Category: Piomelli, D]]
[[Category: Endocannabinoid]]
[[Category: Hydrolase]]
[[Category: Lipase]]

Revision as of 11:06, 26 September 2018

Human N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of Triton X-100Human N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of Triton X-100

Structural highlights

6dxx is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NAAA_HUMAN] Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine.[1]

References

  1. ↑ Tsuboi K, Sun YX, Okamoto Y, Araki N, Tonai T, Ueda N. Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase. J Biol Chem. 2005 Mar 25;280(12):11082-92. Epub 2005 Jan 17. PMID:15655246 doi:http://dx.doi.org/M413473200

6dxx, resolution 2.70Å

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