1an9: Difference between revisions

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-{{Seed}}
-[[Image:1an9.png|left|200px]]
-<!--
+==D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE==
-The line below this paragraph, containing "STRUCTURE_1an9", creates the "Structure Box" on the page.
+<StructureSection load='1an9' size='340' side='right'caption='[[1an9]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1an9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AN9 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-{{STRUCTURE_1an9|  PDB=1an9  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1an9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an9 OCA], [https://pdbe.org/1an9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1an9 RCSB], [https://www.ebi.ac.uk/pdbsum/1an9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1an9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/OXDA_PIG OXDA_PIG] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1an9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1an9 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+As an extension of our recent X-ray crystallographic determination of the tertiary structure of D-amino acid oxidase (DAO) [Mizutani, H. et al. (1996) J. Biochem. 120, 14-17], we solved the crystal structure of the complex of DAO with a substrate analog, o-aminobenzoate (OAB). The alignment between flavin and OAB in the crystal structure of the complex is consistent with charge-transfer interaction through the overlap between the highest occupied molecular orbital of OAB and the lowest unoccupied molecular orbital of flavin. Starting with the atomic coordinates of this complex as the initial model, we carried out molecular mechanics simulation for the DAO-D-leucine complex and thus obtained a model for the enzyme-substrate complex. According to the enzyme-substrate complex model, the alpha-proton is pointed toward N(5) of flavin while the lone-pair of the substrate amino group can approach C(4a) of flavin within an interacting distance. This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism.
-===D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE===
+Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex.,Miura R, Setoyama C, Nishina Y, Shiga K, Mizutani H, Miyahara I, Hirotsu K J Biochem. 1997 Oct;122(4):825-33. PMID:9399588<ref>PMID:9399588</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1an9" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9399588}}, adds the Publication Abstract to the page
+*[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9399588 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9399588}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-AN9 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN9 OCA].
-==Reference==
-<ref group="xtra">PMID:9399588</ref><references group="xtra"/>
-[[Category: D-amino-acid oxidase]]
 [[Category: Sus scrofa]]
-[[Category: Hirotsu, K.]]
+[[Category: Hirotsu K]]
-[[Category: Miura, R.]]
+[[Category: Miura R]]
-[[Category: Miyahara, I.]]
+[[Category: Miyahara I]]
-[[Category: Mizutani, H.]]
+[[Category: Mizutani H]]
-[[Category: Nishina, Y.]]
+[[Category: Nishina Y]]
-[[Category: Setoyama, C.]]
+[[Category: Setoyama C]]
-[[Category: Shiga, K.]]
+[[Category: Shiga K]]
-[[Category: D-amino acid]]
-[[Category: Fad]]
-[[Category: Flavoprotein]]
-[[Category: Oxidase]]
-[[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:07:10 2009''