2daa

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[[Image:2daa.jpg|left|200px]]<br /><applet load="2daa" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2daa, resolution 2.1&Aring;" />
 
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'''CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY D-CYCLOSERINE'''<br />
 
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==About this Structure==
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==CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY D-CYCLOSERINE==
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2DAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=DCS:'>DCS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/D-amino-acid_transaminase D-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.21 2.6.1.21] Known structural/functional Sites: <scene name='pdbsite=ASA:Active+Site+Containing+Plp+Cofactor+Blocked+w.+Cycloseri+...'>ASA</scene> and <scene name='pdbsite=ASB:Essentially+Identical+To+Asa'>ASB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAA OCA].
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<StructureSection load='2daa' size='340' side='right'caption='[[2daa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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[[Category: Bacillus sp.]]
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== Structural highlights ==
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[[Category: D-amino-acid transaminase]]
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<table><tr><td colspan='2'>[[2daa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._(in:_Bacteria) Bacillus sp. (in: Bacteria)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DAA FirstGlance]. <br>
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[[Category: Single protein]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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[[Category: Chipman, D M.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCS:D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-N,O-CYCLOSERYLAMIDE'>DCS</scene></td></tr>
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[[Category: Peisach, D.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2daa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2daa OCA], [https://pdbe.org/2daa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2daa RCSB], [https://www.ebi.ac.uk/pdbsum/2daa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2daa ProSAT]</span></td></tr>
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[[Category: Ringe, D.]]
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</table>
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[[Category: DCS]]
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== Function ==
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[[Category: aminotransferase]]
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[https://www.uniprot.org/uniprot/DAAA_BACYM DAAA_BACYM] Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.<ref>PMID:2914916</ref> <ref>PMID:9538014</ref>
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[[Category: antibiotic]]
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== Evolutionary Conservation ==
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[[Category: cycloserine]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: pyridoxal phosphate]]
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Check<jmol>
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[[Category: pyridoxamine]]
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<jmolCheckbox>
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[[Category: suicide substrate]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/2daa_consurf.spt"</scriptWhenChecked>
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[[Category: transaminase]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: transferase]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2daa ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:56:43 2008''
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==See Also==
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Chipman DM]]
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[[Category: Peisach D]]
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[[Category: Ringe D]]

Current revision

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY D-CYCLOSERINE

PDB ID 2daa

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