1ege: Difference between revisions
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<StructureSection load='1ege' size='340' side='right'caption='[[1ege]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='1ege' size='340' side='right'caption='[[1ege]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ege]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ege]] is a 4 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=1EGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.7, 1.3.8.8 and 1.3.8.9 1.3.8.7, 1.3.8.8 and 1.3.8.9] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ege FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ege OCA], [https://pdbe.org/1ege PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ege RCSB], [https://www.ebi.ac.uk/pdbsum/1ege PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ege ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[[ | [[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[https://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||