5l76

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Current revision (16:09, 4 October 2023) (edit) (undo)
 
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<StructureSection load='5l76' size='340' side='right'caption='[[5l76]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
<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 with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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://proteopedia.org/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" 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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</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AASS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://proteopedia.org/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='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: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C]]
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[[Category: Arrowsmith C]]
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[[Category: Arruda, P]]
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[[Category: Arruda P]]
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[[Category: Borkowska, O]]
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[[Category: Borkowska O]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Burgess-Brown, N]]
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[[Category: Burgess-Brown N]]
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[[Category: Chalk, R]]
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[[Category: Chalk R]]
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[[Category: Edwards, A]]
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[[Category: Edwards A]]
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[[Category: Goubin, S]]
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[[Category: Goubin S]]
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[[Category: Kopec, J]]
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[[Category: Kopec J]]
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[[Category: Pena, I A]]
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[[Category: Pena IA]]
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[[Category: Rembeza, E]]
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[[Category: Rembeza E]]
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[[Category: Strain-Damerell, C]]
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[[Category: Strain-Damerell C]]
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[[Category: Velupillai, S]]
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[[Category: Velupillai S]]
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[[Category: Yue, W W]]
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[[Category: Yue WW]]
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[[Category: Aass]]
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[[Category: Aminoadipate semialdehyde synthase]]
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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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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