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.


1ado

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ado" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ado, resolution 1.9&Aring;" /> '''FRUCTOSE 1,6-BISPHOSP...)
Current revision (06:29, 7 February 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ado.gif|left|200px]]<br /><applet load="1ado" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ado, resolution 1.9&Aring;" />
 
-
'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE'''<br />
 
-
==Overview==
+
==FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE==
-
The structure of fructose 1,6-bisphosphate aldolase shows three distinct, modes of product binding that are correlated to the disposition of the, C-terminal region and depicts a possible trajectory for product exchange., The structure also indicates binding preference for monobasic triose, phosphates.
+
<StructureSection load='1ado' size='340' side='right'caption='[[1ado]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ado]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADO 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]] 1.9&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</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=1ado FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ado OCA], [https://pdbe.org/1ado PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ado RCSB], [https://www.ebi.ac.uk/pdbsum/1ado PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ado ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ALDOA_RABIT ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.<ref>PMID:17329259</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/1ado_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ado ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1ADO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with SO4 and 13P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ADO OCA].
+
*[[Aldolase 3D structures|Aldolase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase., Blom N, Sygusch J, Nat Struct Biol. 1997 Jan;4(1):36-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8989320 8989320]
+
__TOC__
-
[[Category: Fructose-bisphosphate aldolase]]
+
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Single protein]]
+
[[Category: Blom NS]]
-
[[Category: Blom, N.S.]]
+
[[Category: Sygusch J]]
-
[[Category: Sygusch, J.]]
+
-
[[Category: 13P]]
+
-
[[Category: SO4]]
+
-
[[Category: aldolase]]
+
-
[[Category: glycolysis]]
+
-
[[Category: lyase (aldehyde)]]
+
-
[[Category: schiff base]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:46:46 2007''
+

Current revision

FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE

PDB ID 1ado

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/1ado"
Personal tools