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[[Image:1gpd.png|left|200px]]


{{STRUCTURE_1gpd| PDB=1gpd | SCENE= }}
==STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE==
<StructureSection load='1gpd' size='340' side='right'caption='[[1gpd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homarus_americanus Homarus americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPD 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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1gpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpd OCA], [https://pdbe.org/1gpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpd RCSB], [https://www.ebi.ac.uk/pdbsum/1gpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G3P_HOMAM G3P_HOMAM]
== 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/gp/1gpd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1gpd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An improved electron density map of lobster holo-D-glyceraldehyde-3-phosphate dehydrogenase has been computed to 2.9 A resolution based on two heavy atom isomorphous derivatives. This has been averaged only over the Q molecular 2-fold axis, which is known to be exact in the human holoenzyme. The map showed possible asymmetry between the subunits in which the active centers are closely related across the R axis (that is, between the red and green or between the yellow and blue subunits). A difference map between the electron density of citrate and sulfate-soaked crystals gave further evidence for possible asymmetry. The major differences of electron density between R axis-related subunits appear around the active center and suggest the following interpretations. 1. The conformation of the adenine about the glycosidic bond is the more frequently observed anti with a C-2' endo conformation for the ribose ring in the red and yellow subunits, but is probably syn with a C-3' endo conformation in the green and blue subunits.2. The adenine ribose has its 3'-hydroxyl group hydrogen-bonded to a main chain carbonyl group in the red and yellow subunits but not in the green and blue subunits, as a consequence of the differing ribose conformations. 3. Cysteine-149 is more closely associated with histidine-176 in the green and blue subunits, and appears nearer the nicotinamide in the red and yellow subunits.


===STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE===
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase.,Moras D, Olsen KW, Sabesan MN, Buehner M, Ford GC, Rossmann MG J Biol Chem. 1975 Dec 10;250(23):9137-62. PMID:127793<ref>PMID:127793</ref>


{{ABSTRACT_PUBMED_127793}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1gpd" style="background-color:#fffaf0;"></div>
[[1gpd]] is a 2 chain structure of [[Aldehyde dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Homarus_americanus Homarus americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPD OCA].


==See Also==
==See Also==
*[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]]
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
 
*[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:000127793</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Homarus americanus]]
[[Category: Homarus americanus]]
[[Category: Buehner, M.]]
[[Category: Large Structures]]
[[Category: Ford, G C.]]
[[Category: Buehner M]]
[[Category: Moras, D.]]
[[Category: Ford GC]]
[[Category: Olsen, K W.]]
[[Category: Moras D]]
[[Category: Rossmann, M G.]]
[[Category: Olsen KW]]
[[Category: Sabesan, M N.]]
[[Category: Rossmann MG]]
[[Category: Oxidoreductase]]
[[Category: Sabesan MN]]
Retrieved from "https://proteopedia.org/1gpd"