1h83: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1h83]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H83 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1h83]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H83 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIA:OCTANE+1,8-DIAMINE'>DIA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b37|1b37]], [[1b5q|1b5q]], [[1h81|1h81]], [[1h82|1h82]], [[1h84|1h84]], [[1h86|1h86]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIA:OCTANE+1,8-DIAMINE'>DIA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </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=1h83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h83 OCA], [https://pdbe.org/1h83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h83 RCSB], [https://www.ebi.ac.uk/pdbsum/1h83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h83 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=1h83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h83 OCA], [https://pdbe.org/1h83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h83 RCSB], [https://www.ebi.ac.uk/pdbsum/1h83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h83 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PAO_MAIZE PAO_MAIZE]] Catalyzes the oxidation of the secondary amino group of polyamines (spermine, spermidine and their acetyl derivatives). Plays an important role in the regulation of polyamine intracellular concentration.  
[https://www.uniprot.org/uniprot/PAO1_MAIZE PAO1_MAIZE] Flavoenzyme involved in polyamine back-conversion (PubMed:16331971, Ref.4). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (PubMed:16331971, Ref.4). Plays an important role in the regulation of polyamine intracellular concentration (Probable).<ref>PMID:16331971</ref> <ref>PMID:16331971</ref> <ref>PMID:16331971</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/1h83_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/1h83_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oxidoreductase]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Angelini, R]]
[[Category: Angelini R]]
[[Category: Ascenzi, P]]
[[Category: Ascenzi P]]
[[Category: Binda, C]]
[[Category: Binda C]]
[[Category: Coda, A]]
[[Category: Coda A]]
[[Category: Federico, R]]
[[Category: Federico R]]
[[Category: Mattevi, A]]
[[Category: Mattevi A]]
[[Category: Flavin-dependent amine oxidase]]

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