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3kpf
From Proteopedia
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| - | [[Image:3kpf.png|left|200px]] | ||
| - | + | ==X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays== | |
| - | + | <StructureSection load='3kpf' size='340' side='right'caption='[[3kpf]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3kpf]] 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=3KPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KPF 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]] 2.9Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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></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=3kpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kpf OCA], [https://pdbe.org/3kpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kpf RCSB], [https://www.ebi.ac.uk/pdbsum/3kpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kpf ProSAT]</span></td></tr> |
| - | [[3kpf]] is a 2 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PAO1_MAIZE PAO1_MAIZE] Flavoenzyme involved in polyamine back-conversion (Ref.4, PubMed:16331971). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (Ref.4, PubMed:16331971). 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== | ==See Also== | ||
*[[Polyamine oxidase|Polyamine oxidase]] | *[[Polyamine oxidase|Polyamine oxidase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
| - | [[Category: Fiorillo | + | [[Category: Fiorillo A]] |
| - | [[Category: Ilari | + | [[Category: Ilari A]] |
| - | [[Category: Tavladoraki | + | [[Category: Tavladoraki P]] |
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Current revision
X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays
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