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
Current revision (06:29, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ado.gif|left|200px]]
 
-
{{Structure
+
==FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE==
-
|PDB= 1ado |SIZE=350|CAPTION= <scene name='initialview01'>1ado</scene>, resolution 1.9&Aring;
+
<StructureSection load='1ado' size='340' side='right'caption='[[1ado]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>
+
<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>
-
|ACTIVITY= [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]
+
</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>
-
|GENE=
+
<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>
-
'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE'''
+
==See Also==
-
 
+
*[[Aldolase 3D structures|Aldolase 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
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.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1ADO is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==Reference==
+
-
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://www.ncbi.nlm.nih.gov/pubmed/8989320 8989320]
+
-
[[Category: Fructose-bisphosphate aldolase]]
+
[[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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:05 2008''
+

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

Personal tools