2pqt

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[[Image:2pqt.gif|left|200px]]<br /><applet load="2pqt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pqt.gif|left|200px]]
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caption="2pqt, resolution 1.780&Aring;" />
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'''Human N-acetyltransferase 1'''<br />
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{{Structure
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|PDB= 2pqt |SIZE=350|CAPTION= <scene name='initialview01'>2pqt</scene>, resolution 1.780&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=UNX:UNKNOWN ATOM OR ION'>UNX</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Arylamine_N-acetyltransferase Arylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.5 2.3.1.5]
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|GENE= NAT1, AAC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Human N-acetyltransferase 1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PQT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arylamine_N-acetyltransferase Arylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.5 2.3.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQT OCA].
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2PQT is a [[Single protein]] structure of 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=2PQT OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17656365 17656365]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17656365 17656365]
[[Category: Arylamine N-acetyltransferase]]
[[Category: Arylamine N-acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: structural genomics consortium]]
[[Category: structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:18 2008''

Revision as of 16:16, 20 March 2008

Image:2pqt.gif


PDB ID 2pqt

Drag the structure with the mouse to rotate
, resolution 1.780Å
Ligands: and
Gene: NAT1, AAC1 (Homo sapiens)
Activity: Arylamine N-acetyltransferase, with EC number 2.3.1.5
Coordinates: save as pdb, mmCIF, xml



Human N-acetyltransferase 1


Contents

Overview

The 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.

Disease

Known disease associated with this structure: Orthostatic intolerance OMIM:[163970]

About this Structure

2PQT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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