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==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.== | ==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.== | ||
<StructureSection load='5o1o' size='340' side='right' caption='[[5o1o]], [[Resolution|resolution]] 2.48Å' scene=''> | <StructureSection load='5o1o' size='340' side='right'caption='[[5o1o]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o1o]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5o1o]] is a 2 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=5O1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O1O FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48Å</td></tr> | ||
<tr id=' | <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=PRO:PROLINE'>PRO</scene></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=5o1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1o OCA], [https://pdbe.org/5o1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o1o RCSB], [https://www.ebi.ac.uk/pdbsum/5o1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [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 == | ||
[ | [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> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith | [[Category: Large Structures]] | ||
[[Category: Arruda | [[Category: Arrowsmith C]] | ||
[[Category: Bountra | [[Category: Arruda P]] | ||
[[Category: Burgess-Brown | [[Category: Bountra C]] | ||
[[Category: Collins | [[Category: Burgess-Brown N]] | ||
[[Category: Collins P]] | |||
[[Category: Edwards | [[Category: Edwards A]] | ||
[[Category: Goubin | [[Category: Goubin S]] | ||
[[Category: Kopec | [[Category: Kopec J]] | ||
[[Category: Krojer | [[Category: Krojer T]] | ||
[[Category: Kupinska | [[Category: Kupinska K]] | ||
[[Category: Mathea | [[Category: Mathea S]] | ||
[[Category: Pena | [[Category: Pena IA]] | ||
[[Category: Rembeza | [[Category: Rembeza E]] | ||
[[Category: Strain-Damerell | [[Category: Strain-Damerell C]] | ||
[[Category: Talon | [[Category: Talon R]] | ||
[[Category: Velupillai | [[Category: Velupillai S]] | ||
[[Category: Yue | [[Category: Yue WW]] | ||
[[Category: | [[Category: Von Delft F]] | ||
Latest revision as of 22:03, 29 November 2023
Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.
Structural highlights
DiseaseAASS_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.[1] FunctionAASS_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
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