5o1o

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m (Protected "5o1o" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5o1o is ON HOLD
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==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.==
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<StructureSection load='5o1o' size='340' side='right'caption='[[5o1o]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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Authors: Kopec, J., Rembeza, E., Pena, I.A., Mathea, S., Velupillai, S., Strain-Damerell, C., Goubin, S., Kupinska, K., Talon, R., Collins, P., Krojer, T., Burgess-Brown, N., Arrowsmith, C., Edwards, A., Bountra, C., von Delft, F., Arruda, P., Yue, W.W.
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== Structural highlights ==
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<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>
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Description: Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.
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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]] 2.48&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=PRO:PROLINE'>PRO</scene></td></tr>
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[[Category: Goubin, S]]
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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=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>
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[[Category: Collins, P]]
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</table>
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[[Category: Mathea, S]]
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== Disease ==
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[[Category: Burgess-Brown, N]]
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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>
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[[Category: Velupillai, S]]
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== Function ==
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[[Category: Yue, W.W]]
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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.
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[[Category: Kopec, J]]
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== References ==
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[[Category: Von Delft, F]]
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<references/>
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[[Category: Arrowsmith, C]]
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__TOC__
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[[Category: Talon, R]]
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</StructureSection>
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[[Category: Arruda, P]]
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[[Category: Homo sapiens]]
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[[Category: Pena, I.A]]
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[[Category: Large Structures]]
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[[Category: Edwards, A]]
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[[Category: Arrowsmith C]]
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[[Category: Strain-Damerell, C]]
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[[Category: Arruda P]]
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[[Category: Krojer, T]]
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[[Category: Bountra C]]
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[[Category: Rembeza, E]]
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[[Category: Burgess-Brown N]]
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[[Category: Bountra, C]]
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[[Category: Collins P]]
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[[Category: Kupinska, K]]
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[[Category: Edwards A]]
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[[Category: Goubin S]]
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[[Category: Kopec J]]
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[[Category: Krojer T]]
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[[Category: Kupinska K]]
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[[Category: Mathea S]]
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[[Category: Pena IA]]
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[[Category: Rembeza E]]
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[[Category: Strain-Damerell C]]
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[[Category: Talon R]]
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[[Category: Velupillai S]]
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[[Category: Yue WW]]
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[[Category: Von Delft F]]

Current revision

Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.

PDB ID 5o1o

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