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2cg5
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cg5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CG5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CG5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2cg5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CG5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CG5 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2byd|2byd]], [[2c43|2c43]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2byd|2byd]], [[2c43|2c43]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cg5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cg5 RCSB], [http://www.ebi.ac.uk/pdbsum/2cg5 PDBsum]</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=2cg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cg5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cg5 RCSB], [http://www.ebi.ac.uk/pdbsum/2cg5 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: L-aminoadipate-semialdehyde dehydrogenase]] | [[Category: L-aminoadipate-semialdehyde dehydrogenase]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C]] |
| - | [[Category: Bunkoczi, G | + | [[Category: Bunkoczi, G]] |
| - | [[Category: Delft, F Von | + | [[Category: Delft, F Von]] |
| - | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
| - | [[Category: Joshi, A | + | [[Category: Joshi, A]] |
| - | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
| - | [[Category: Papagrigoriu, E | + | [[Category: Papagrigoriu, E]] |
| - | [[Category: Smith, S | + | [[Category: Smith, S]] |
| - | [[Category: Sundstrom, M | + | [[Category: Sundstrom, M]] |
| - | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
[[Category: Acp]] | [[Category: Acp]] | ||
[[Category: Coenzyme some]] | [[Category: Coenzyme some]] | ||
Revision as of 08:01, 25 December 2014
STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL CARRIER PROTEIN AND COENZYME A
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Categories: Homo sapiens | L-aminoadipate-semialdehyde dehydrogenase | Arrowsmith, C | Bunkoczi, G | Delft, F Von | Edwards, A | Joshi, A | Oppermann, U | Papagrigoriu, E | Smith, S | Sundstrom, M | Weigelt, J | Acp | Coenzyme some | Complex | Fasn | Fatty acid biosynthesis | Hydrolase | Lipid synthesis | Lyase | Phosphopantetheine transferase | Transferase | Transferase-hydrolase complex
