5l76

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==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain (in apo form)==
==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain (in apo form)==
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<StructureSection load='5l76' size='340' side='right' caption='[[5l76]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
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<StructureSection load='5l76' size='340' side='right'caption='[[5l76]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5l76]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L76 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5l76]] 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=5L76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L76 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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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]] 2.57&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l76 OCA], [http://pdbe.org/5l76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l76 RCSB], [http://www.ebi.ac.uk/pdbsum/5l76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l76 ProSAT]</span></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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5l76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l76 OCA], [https://pdbe.org/5l76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l76 RCSB], [https://www.ebi.ac.uk/pdbsum/5l76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l76 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/AASS_HUMAN AASS_HUMAN]] Hyperlysinemia;Saccharopinuria. The disease is caused by mutations affecting the gene represented in this entry. The protein represented in this entry is involved in disease pathogenesis. A selective decrease in mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS.<ref>PMID:24847004</ref>
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[https://www.uniprot.org/uniprot/AASS_HUMAN AASS_HUMAN] Hyperlysinemia;Saccharopinuria. The disease is caused by mutations affecting the gene represented in this entry. The protein represented in this entry is involved in disease pathogenesis. A selective decrease in mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS.<ref>PMID:24847004</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AASS_HUMAN AASS_HUMAN]] Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively.
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[https://www.uniprot.org/uniprot/AASS_HUMAN AASS_HUMAN] Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively.
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arrowsmith, C]]
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[[Category: Homo sapiens]]
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[[Category: Arruda, P]]
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[[Category: Large Structures]]
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[[Category: Borkowska, O]]
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[[Category: Arrowsmith C]]
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[[Category: Bountra, C]]
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[[Category: Arruda P]]
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[[Category: Burgess-Brown, N]]
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[[Category: Borkowska O]]
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[[Category: Chalk, R]]
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[[Category: Bountra C]]
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[[Category: Edwards, A]]
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[[Category: Burgess-Brown N]]
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[[Category: Goubin, S]]
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[[Category: Chalk R]]
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[[Category: Kopec, J]]
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[[Category: Edwards A]]
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[[Category: Pena, I A]]
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[[Category: Goubin S]]
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[[Category: Rembeza, E]]
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[[Category: Kopec J]]
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[[Category: Strain-Damerell, C]]
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[[Category: Pena IA]]
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[[Category: Velupillai, S]]
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[[Category: Rembeza E]]
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[[Category: Yue, W W]]
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[[Category: Strain-Damerell C]]
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[[Category: Aass]]
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[[Category: Velupillai S]]
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[[Category: Aminoadipate semialdehyde synthase]]
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[[Category: Yue WW]]
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[[Category: Oxidoreductase]]
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[[Category: Sdh]]
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Current revision

Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain (in apo form)

PDB ID 5l76

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