5o1n
From Proteopedia
(Difference between revisions)
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==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with N-[(2S)-2-Pyrrolidinylmethyl]-trifluoromethanesulfonamide bound== | ==Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with N-[(2S)-2-Pyrrolidinylmethyl]-trifluoromethanesulfonamide bound== | ||
| - | <StructureSection load='5o1n' size='340' side='right' caption='[[5o1n]], [[Resolution|resolution]] 2.28Å' scene=''> | + | <StructureSection load='5o1n' size='340' side='right'caption='[[5o1n]], [[Resolution|resolution]] 2.28Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5o1n]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5o1n]] 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=5O1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O1N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9H8:1,1,1-tris(fluoranyl)-~{N}-[[(2~{S})-pyrrolidin-2-yl]methyl]methanesulfonamide'>9H8</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9H8:1,1,1-tris(fluoranyl)-~{N}-[[(2~{S})-pyrrolidin-2-yl]methyl]methanesulfonamide'>9H8</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5o1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o1n OCA], [https://pdbe.org/5o1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o1n RCSB], [https://www.ebi.ac.uk/pdbsum/5o1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o1n 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: Brennan | + | [[Category: Bountra C]] |
| - | [[Category: Burgess-Brown | + | [[Category: Brennan P]] |
| - | [[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: McLaughlin | + | [[Category: McLaughlin M]] |
| - | [[Category: Pena | + | [[Category: Pena IA]] |
| - | [[Category: Rembeza | + | [[Category: Rembeza E]] |
| - | [[Category: Sethi | + | [[Category: Sethi R]] |
| - | [[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]] |
| - | + | ||
Current revision
Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with N-[(2S)-2-Pyrrolidinylmethyl]-trifluoromethanesulfonamide bound
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Categories: Homo sapiens | Large Structures | Arrowsmith C | Arruda P | Bountra C | Brennan P | Burgess-Brown N | Collins P | Edwards A | Goubin S | Kopec J | Krojer T | McLaughlin M | Pena IA | Rembeza E | Sethi R | Strain-Damerell C | Talon R | Velupillai S | Yue WW | Von Delft F
