5o1o: Difference between revisions
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==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5o1o]] is a 2 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=5O1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O1O FirstGlance]. <br> | |||
</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=PRO:PROLINE'>PRO</scene></td></tr> | |||
[[ | <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> | ||
[[ | <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=5o1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1o OCA], [http://pdbe.org/5o1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o1o RCSB], [http://www.ebi.ac.uk/pdbsum/5o1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1o ProSAT]</span></td></tr> | ||
[[ | </table> | ||
[[ | == Disease == | ||
[[ | [[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> | ||
[[ | == Function == | ||
[[ | [[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. | ||
[[ | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Arrowsmith, C]] | [[Category: Arrowsmith, C]] | ||
[[Category: Arruda, P]] | [[Category: Arruda, P]] | ||
[[Category: | [[Category: Bountra, C]] | ||
[[Category: Burgess-Brown, N]] | |||
[[Category: Collins, P]] | |||
[[Category: Delft, F von]] | |||
[[Category: Edwards, A]] | [[Category: Edwards, A]] | ||
[[Category: | [[Category: Goubin, S]] | ||
[[Category: Kopec, J]] | |||
[[Category: Krojer, T]] | [[Category: Krojer, T]] | ||
[[Category: Kupinska, K]] | |||
[[Category: Mathea, S]] | |||
[[Category: Pena, I A]] | |||
[[Category: Rembeza, E]] | [[Category: Rembeza, E]] | ||
[[Category: | [[Category: Strain-Damerell, C]] | ||
[[Category: | [[Category: Talon, R]] | ||
[[Category: Velupillai, S]] | |||
[[Category: Yue, W W]] | |||
[[Category: Human aminoadipate semialdehyde synthase]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Sdr]] | |||
Revision as of 14:10, 6 November 2017
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
Disease[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.[1] Function[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
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