This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5mbx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (18:37, 1 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of reduced murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine==
==Crystal structure of reduced murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine==
-
<StructureSection load='5mbx' size='340' side='right' caption='[[5mbx]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+
<StructureSection load='5mbx' size='340' side='right'caption='[[5mbx]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5mbx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MBX FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5mbx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MBX FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SP5:N-[3-({4-[(3-AMINOPROPYL)AMINO]BUTYL}AMINO)PROPYL]ACETAMIDE'>SP5</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(1)-acetylpolyamine_oxidase N(1)-acetylpolyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13 1.5.3.13] </span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SP5:N-[3-({4-[(3-AMINOPROPYL)AMINO]BUTYL}AMINO)PROPYL]ACETAMIDE'>SP5</scene></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mbx OCA], [http://pdbe.org/5mbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mbx RCSB], [http://www.ebi.ac.uk/pdbsum/5mbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mbx 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=5mbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mbx OCA], [https://pdbe.org/5mbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mbx RCSB], [https://www.ebi.ac.uk/pdbsum/5mbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mbx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PAOX_MOUSE PAOX_MOUSE]] Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. 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.
+
[https://www.uniprot.org/uniprot/PAOX_MOUSE PAOX_MOUSE] Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 23: Line 23:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Aagaard, A]]
+
[[Category: Large Structures]]
-
[[Category: Barlind, L]]
+
[[Category: Mus musculus]]
-
[[Category: Sjogren, T]]
+
[[Category: Aagaard A]]
-
[[Category: Snijder, A]]
+
[[Category: Barlind L]]
-
[[Category: Wassvik, C]]
+
[[Category: Sjogren T]]
-
[[Category: Flavin amine oxidase]]
+
[[Category: Snijder A]]
-
[[Category: Oxidoreductase]]
+
[[Category: Wassvik C]]

Current revision

Crystal structure of reduced murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine

PDB ID 5mbx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5mbx"
Personal tools