2pqt: Difference between revisions
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<StructureSection load='2pqt' size='340' side='right'caption='[[2pqt]], [[Resolution|resolution]] 1.78Å' scene=''> | <StructureSection load='2pqt' size='340' side='right'caption='[[2pqt]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pqt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2pqt]] 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=2PQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78Å</td></tr> | ||
<tr id=' | <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=TYX:S-(2-ANILINO-2-OXOETHYL)-L-CYSTEINE'>TYX</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=2pqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqt OCA], [https://pdbe.org/2pqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqt RCSB], [https://www.ebi.ac.uk/pdbsum/2pqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqt 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=2pqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqt OCA], [https://pdbe.org/2pqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqt RCSB], [https://www.ebi.ac.uk/pdbsum/2pqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ARY1_HUMAN ARY1_HUMAN] Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Bochkarev | [[Category: Bochkarev A]] | ||
[[Category: Dombrovski | [[Category: Dombrovski L]] | ||
[[Category: Edwards | [[Category: Edwards AM]] | ||
[[Category: Grant | [[Category: Grant DM]] | ||
[[Category: Loppnau | [[Category: Loppnau P]] | ||
[[Category: Plotnikov | [[Category: Plotnikov AN]] | ||
[[Category: Sundstrom M]] | |||
[[Category: Sundstrom | [[Category: Tempel W]] | ||
[[Category: Tempel | [[Category: Weigelt J]] | ||
[[Category: Weigelt | [[Category: Wu H]] | ||
[[Category: Wu | |||
Latest revision as of 14:07, 30 August 2023
Human N-acetyltransferase 1Human N-acetyltransferase 1
Structural highlights
FunctionARY1_HUMAN Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe human arylamine N-acetyltransferases NAT1 and NAT2 play an important role in the biotransformation of a plethora of aromatic amine and hydrazine drugs. They are also able to participate in the bioactivation of several known carcinogens. Each of these enzymes is genetically variable in human populations, and polymorphisms in NAT genes have been associated with various cancers. Here we have solved the high resolution crystal structures of human NAT1 and NAT2, including NAT1 in complex with the irreversible inhibitor 2-bromoacetanilide, a NAT1 active site mutant, and NAT2 in complex with CoA, and have refined them to 1.7-, 1.8-, and 1.9-A resolution, respectively. The crystal structures reveal novel structural features unique to human NATs and provide insights into the structural basis of the substrate specificity and genetic polymorphism of these enzymes. Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases.,Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. PMID:17656365[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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