7oy0
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7oy0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OY0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7oy0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OY0 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3EI:4-[(4-imidazo[1,2-a]pyridin-3-yl-1,3-thiazol-2-yl)amino]phenol'>3EI</scene>, <scene name='pdbligand=6YU: | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3EI:4-[(4-imidazo[1,2-a]pyridin-3-yl-1,3-thiazol-2-yl)amino]phenol'>3EI</scene>, <scene name='pdbligand=6YU:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2~{R},3~{S},4~{S})-5-[5-[(~{E})-4-[4-(buta-2,3-dienylamino)butylimino]but-2-en-2-yl]-7,8-dimethyl-2,4-bis(oxidanylidene)-1~{H}-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl]+hydrogen+phosphate'>6YU</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=7oy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oy0 OCA], [https://pdbe.org/7oy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oy0 RCSB], [https://www.ebi.ac.uk/pdbsum/7oy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oy0 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=7oy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oy0 OCA], [https://pdbe.org/7oy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oy0 RCSB], [https://www.ebi.ac.uk/pdbsum/7oy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oy0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SMOX_HUMAN SMOX_HUMAN] Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal. | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Current revision
Structure of human Spermine Oxidase in complex with a highly selective allosteric inhibitor
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