5d6b: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5d6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D6B FirstGlance]. <br>
<table><tr><td colspan='2'>[[5d6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D6B FirstGlance]. <br>
</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=5d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6b OCA], [https://pdbe.org/5d6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d6b RCSB], [https://www.ebi.ac.uk/pdbsum/5d6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d6b ProSAT]</span></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]] 2.1&#8491;</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=5d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6b OCA], [https://pdbe.org/5d6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d6b RCSB], [https://www.ebi.ac.uk/pdbsum/5d6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d6b ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN] Also acts as a tumor suppressor.
[https://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN] Also acts as a tumor suppressor.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human fumarase (HsFH) is a well-known citric acid cycle enzyme and is therefore a key component in energy metabolism. Genetic studies on human patients have shown that polymorphisms in the fumarase gene are responsible for diseases such as hereditary leiomyomatosis and renal cell cancer. As a first step in unravelling the molecular basis of the mechanism of fumarase deficiency in genetic disorders, the HsFH gene was cloned in pET-28a, heterologously expressed in Escherichia coli, purified by nickel-affinity chromatography and crystallized using the vapour-diffusion technique. X-ray diffraction experiments were performed at a synchrotron source and the structure was solved at 2.1 A resolution by molecular replacement.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of recombinant human fumarase.,Pereira de Padua RA, Nonato MC Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):120-2. doi:, 10.1107/S2053230X13033955. Epub 2013 Dec 24. PMID:24419633<ref>PMID:24419633</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5d6b" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 12:23, 6 March 2024

Human fumarase (wild type)

5d6b, resolution 2.10Å

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