2r0m: Difference between revisions

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<StructureSection load='2r0m' size='340' side='right'caption='[[2r0m]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2r0m' size='340' side='right'caption='[[2r0m]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2r0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R0M FirstGlance]. <br>
<table><tr><td colspan='2'>[[2r0m]] 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=2R0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R0M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NI:4-NITROBUTANOIC+ACID'>4NI</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r0n|2r0n]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NI:4-NITROBUTANOIC+ACID'>4NI</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutaryl-CoA_dehydrogenase_(ETF) Glutaryl-CoA dehydrogenase (ETF)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.6 1.3.8.6] </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=2r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0m OCA], [https://pdbe.org/2r0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r0m RCSB], [https://www.ebi.ac.uk/pdbsum/2r0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0m ProSAT]</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=2r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0m OCA], [https://pdbe.org/2r0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r0m RCSB], [https://www.ebi.ac.uk/pdbsum/2r0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0m ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/GCDH_HUMAN GCDH_HUMAN]] Defects in GCDH are the cause of glutaric aciduria type 1 (GA1) [MIM:[https://omim.org/entry/231670 231670]]. GA1 is an autosomal recessive metabolic disorder characterized by progressive dystonia and athetosis due to gliosis and neuronal loss in the basal ganglia.<ref>PMID:18775954</ref> <ref>PMID:8541831</ref> <ref>PMID:9600243</ref> <ref>PMID:8900227</ref> <ref>PMID:8900228</ref> <ref>PMID:14707522</ref>
[https://www.uniprot.org/uniprot/GCDH_HUMAN GCDH_HUMAN] Defects in GCDH are the cause of glutaric aciduria type 1 (GA1) [MIM:[https://omim.org/entry/231670 231670]. GA1 is an autosomal recessive metabolic disorder characterized by progressive dystonia and athetosis due to gliosis and neuronal loss in the basal ganglia.<ref>PMID:18775954</ref> <ref>PMID:8541831</ref> <ref>PMID:9600243</ref> <ref>PMID:8900227</ref> <ref>PMID:8900228</ref> <ref>PMID:14707522</ref>  
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GCDH_HUMAN GCDH_HUMAN]] Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive.  
[https://www.uniprot.org/uniprot/GCDH_HUMAN GCDH_HUMAN] Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Albro, M]]
[[Category: Albro M]]
[[Category: Baddam, S]]
[[Category: Baddam S]]
[[Category: Frerman, F E]]
[[Category: Frerman FE]]
[[Category: Fu, Z]]
[[Category: Fu Z]]
[[Category: Kim, J J]]
[[Category: Kim JJ]]
[[Category: Lee, H J]]
[[Category: Lee HJ]]
[[Category: Narayanan, B]]
[[Category: Narayanan B]]
[[Category: Rao, K S]]
[[Category: Rao KS]]
[[Category: Alternative splicing]]
[[Category: Disease mutation]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Glutaryl-coa dehydrogenase]]
[[Category: Isomerase]]
[[Category: Mitochondrion]]
[[Category: Oxidoreductase]]
[[Category: Polymorphism]]
[[Category: Transit peptide]]
Retrieved from "https://proteopedia.org/2r0m"