3kpf: Difference between revisions

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[[Image:3kpf.png|left|200px]]


{{STRUCTURE_3kpf|  PDB=3kpf  |  SCENE=  }}
==X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays==
 
<StructureSection load='3kpf' size='340' side='right'caption='[[3kpf]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
===X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays===
== 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>
{{ABSTRACT_PUBMED_021205212}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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>
==About this Structure==
<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 of [[Polyamine oxidase]] with sequence from [http://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].  
</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==
==See Also==
*[[Polyamine oxidase|Polyamine oxidase]]
*[[Polyamine oxidase|Polyamine oxidase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021205212</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Fiorillo, A.]]
[[Category: Fiorillo A]]
[[Category: Ilari, A.]]
[[Category: Ilari A]]
[[Category: Tavladoraki, P.]]
[[Category: Tavladoraki P]]
[[Category: Disulfide bond]]
[[Category: Fad]]
[[Category: Flavoenzyme]]
[[Category: Flavoprotein]]
[[Category: Glycoprotein]]
[[Category: Oxidoreductase]]
[[Category: Polyamine oxidase]]

Latest revision as of 12:21, 30 October 2024

X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea maysX-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays

Structural highlights

3kpf is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

See Also

References

  1. ↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
  2. ↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
  3. ↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i

3kpf, resolution 2.90Å

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