5c37
From Proteopedia
(Difference between revisions)
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==Structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor== | ==Structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor== | ||
- | <StructureSection load='5c37' size='340' side='right' caption='[[5c37]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5c37' size='340' side='right'caption='[[5c37]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5c37]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C37 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c37]] 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=5C37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C37 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4XN:6-{[(3R)-1-(CYCLOPROPYLCARBONYL)PYRROLIDIN-3-YL]METHYL}-5-[4-(1-METHYL-1H-INDAZOL-5-YL)PHENYL]-4,6-DIAZASPIRO[2.4]HEPT-4-EN-7-ONE'>4XN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4XN:6-{[(3R)-1-(CYCLOPROPYLCARBONYL)PYRROLIDIN-3-YL]METHYL}-5-[4-(1-METHYL-1H-INDAZOL-5-YL)PHENYL]-4,6-DIAZASPIRO[2.4]HEPT-4-EN-7-ONE'>4XN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FASN, FAS ([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=5c37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c37 OCA], [http://pdbe.org/5c37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c37 RCSB], [http://www.ebi.ac.uk/pdbsum/5c37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c37 ProSAT]</span></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=5c37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c37 OCA], [http://pdbe.org/5c37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c37 RCSB], [http://www.ebi.ac.uk/pdbsum/5c37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c37 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. | [[http://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Grasberger, B]] | [[Category: Grasberger, B]] | ||
[[Category: Milligan, C M]] | [[Category: Milligan, C M]] |
Revision as of 11:10, 18 March 2020
Structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor
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