View source for 6sbi


==X-ray structure of murine Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate==
<StructureSection load='6sbi' size='340' side='right'caption='[[6sbi]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6sbi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SBI 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</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=6sbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sbi OCA], [https://pdbe.org/6sbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sbi RCSB], [https://www.ebi.ac.uk/pdbsum/6sbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sbi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FAHD1_MOUSE FAHD1_MOUSE] Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). Also has oxaloacetate decarboxylase activity (PubMed:25575590).[UniProtKB:Q6P587]<ref>PMID:25575590</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.

Structural and Functional Comparison of Fumarylacetoacetate Domain Containing Protein 1 (FAHD1) in Human and Mouse.,Weiss AKH, Naschberger A, Cappuccio E, Metzger C, Mottes L, Holzknecht M, von Velsen J, Bowler MW, Rupp B, Jansen-Durr P Biosci Rep. 2020 Feb 18. pii: 222164. doi: 10.1042/BSR20194431. PMID:32068790<ref>PMID:32068790</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6sbi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Naschberger A]]
[[Category: Rupp B]]
[[Category: Weiss AKH]]