3kpf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 3kpf is ON HOLD  until Paper Publication
==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=''>
== 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]] 2.9&#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>
<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>
</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>


Authors: Fiorillo, A., Ilari, A., Tavladoraki, P.
==See Also==
 
*[[Polyamine oxidase|Polyamine oxidase]]
Description: X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays
== References ==
 
<references/>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec  2 09:38:57 2009''
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Fiorillo A]]
[[Category: Ilari A]]
[[Category: Tavladoraki P]]

Latest revision as of 09:21, 30 October 2024

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

3kpf, resolution 2.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA