1oat: Difference between revisions
New page: left|200px<br /> <applet load="1oat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oat, resolution 2.5Å" /> '''ORNITHINE AMINOTRANS... |
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==About this Structure== | ==About this Structure== | ||
1OAT 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 PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.13 2.6.1.13]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAT OCA]]. | 1OAT 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 PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Ornithine_aminotransferase Ornithine aminotransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.13 2.6.1.13]]. Structure known Active Sites: PLA, PLB and PLC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAT OCA]]. | ||
==Reference== | ==Reference== | ||
Crystal structure of human recombinant ornithine aminotransferase., Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T, J Mol Biol. 1998 Mar 20;277(1):81-102. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9514741 9514741] | Crystal structure of human recombinant ornithine aminotransferase., Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T, J Mol Biol. 1998 Mar 20;277(1):81-102. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9514741 9514741] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ornithine aminotransferase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jansonius, J.N.]] | [[Category: Jansonius, J.N.]] | ||
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[[Category: pyridoxal phosphate]] | [[Category: pyridoxal phosphate]] | ||
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Revision as of 13:49, 30 October 2007
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ORNITHINE AMINOTRANSFERASE
OverviewOverview
Ornithine aminotransferase (OAT), a pyridoxal-5'-phosphate dependent, enzyme, catalyses the transfer of the delta-amino group of L-ornithine to, 2-oxoglutarate, producing L-glutamate-gamma-semialdehyde, which, spontaneously cyclizes to pyrroline-5-carboxylate, and L-glutamate. The, crystal structure determination of human recombinant OAT is described in, this paper. As a first step, the structure was determined at low, resolution (6 A) by molecular replacement using the refined structure of, dialkylglycine decarboxylase as a search model. Crystallographic phases, were then refined and extended in a step-wise fashion to 2.5 A by cyclic, averaging of the electron density corresponding to the three monomers, within the asymmetric unit. Interpretation of the resulting map was, straightforward ... [(full description)]
About this StructureAbout this Structure
1OAT is a [Single protein] structure of sequence from [Homo sapiens] with PLP as [ligand]. Active as [Ornithine aminotransferase], with EC number [2.6.1.13]. Structure known Active Sites: PLA, PLB and PLC. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of human recombinant ornithine aminotransferase., Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T, J Mol Biol. 1998 Mar 20;277(1):81-102. PMID:9514741
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