4ldk

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'''Unreleased structure'''
 
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The entry 4ldk is ON HOLD until Paper Publication
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==FAD-linked sulfhydryl oxidase ALR mutation==
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<StructureSection load='4ldk' size='340' side='right'caption='[[4ldk]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ldk]] 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=4LDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LDK FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ldk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ldk OCA], [https://pdbe.org/4ldk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ldk RCSB], [https://www.ebi.ac.uk/pdbsum/4ldk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ldk ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref>
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Authors: Dong, M., Ramadan, S., Thorpe, C., Bahnson, B.
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==See Also==
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*[[Sulfhydryl oxidase 3D structures|Sulfhydryl oxidase 3D structures]]
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Description: FAD-linked sulfhydryl oxidase ALR mutation
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Bahnson B]]
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[[Category: Dong M]]
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[[Category: Ramadan S]]
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[[Category: Thorpe C]]

Current revision

FAD-linked sulfhydryl oxidase ALR mutation

PDB ID 4ldk

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