3ku9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine== | |
| + | <StructureSection load='3ku9' size='340' side='right'caption='[[3ku9]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ku9]] is a 2 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=3KU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KU9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</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=3ku9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ku9 OCA], [https://pdbe.org/3ku9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ku9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ku9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ku9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| - | + | ==See Also== | |
| - | + | *[[Polyamine oxidase|Polyamine oxidase]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Zea mays]] | ||
| + | [[Category: Fiorillo A]] | ||
| + | [[Category: Ilari A]] | ||
| + | [[Category: Tavladoraki P]] | ||
Current revision
X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine
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