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==Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle==
==Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle==
<StructureSection load='5f4x' size='340' side='right' caption='[[5f4x]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='5f4x' size='340' side='right'caption='[[5f4x]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5f4x]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F4X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F4X FirstGlance]. <br>
<table><tr><td colspan='2'>[[5f4x]] 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=5F4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F4X FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.84&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2g|5f2g]], [[5f2i|5f2i]], [[5f2j|5f2j]], [[5f2l|5f2l]], [[5f2m|5f2m]], [[5f4s|5f4s]], [[5f4w|5f4w]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=5f4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f4x OCA], [https://pdbe.org/5f4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f4x RCSB], [https://www.ebi.ac.uk/pdbsum/5f4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f4x ProSAT]</span></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=5f4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f4x OCA], [http://pdbe.org/5f4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f4x RCSB], [http://www.ebi.ac.uk/pdbsum/5f4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f4x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
 
==See Also==
*[[Aldolase 3D structures|Aldolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Large Structures]]
[[Category: Arthus-Cartier, G]]
[[Category: Oryctolagus cuniculus]]
[[Category: LowKam, C]]
[[Category: Arthus-Cartier G]]
[[Category: Aldolase]]
[[Category: LowKam C]]
[[Category: Class i]]
[[Category: Lyase]]
[[Category: Lysine mutant]]

Latest revision as of 11:46, 12 July 2023

Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscleFructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle

Structural highlights

5f4x is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.84Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALDOA_RABIT Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]

See Also

References

  1. ↑ St-Jean M, Izard T, Sygusch J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. J Biol Chem. 2007 May 11;282(19):14309-15. Epub 2007 Feb 27. PMID:17329259 doi:10.1074/jbc.M611505200

5f4x, resolution 1.84Å

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