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.


5lgb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:59, 11 October 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of murine N1-acetylpolyamine oxidase in complex with MDL72527==
==Crystal structure of murine N1-acetylpolyamine oxidase in complex with MDL72527==
-
<StructureSection load='5lgb' size='340' side='right' caption='[[5lgb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='5lgb' size='340' side='right'caption='[[5lgb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5lgb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LGB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LGB FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5lgb]] 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=5LGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LGB FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6YU:FAD-MDL72527+adduct'>6YU</scene>, <scene name='pdbligand=MD2:N,N-BIS(2,3-BUTADIENYL)-1,4-BUTANE-DIAMINE'>MD2</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]] 1.8&#8491;</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=5lgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgb OCA], [http://pdbe.org/5lgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lgb RCSB], [http://www.ebi.ac.uk/pdbsum/5lgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgb ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6YU:FAD-MDL72527+adduct'>6YU</scene>, <scene name='pdbligand=MD2:N,N-BIS(2,3-BUTADIENYL)-1,4-BUTANE-DIAMINE'>MD2</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=5lgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgb OCA], [https://pdbe.org/5lgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lgb RCSB], [https://www.ebi.ac.uk/pdbsum/5lgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgb 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 22: 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 murine N1-acetylpolyamine oxidase in complex with MDL72527

PDB ID 5lgb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools