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4d7z
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==E. coli L-aspartate-alpha-decarboxylase mutant N72Q to a resolution of 1.9 Angstroms== |
| - | + | <StructureSection load='4d7z' size='340' side='right' caption='[[4d7z]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4d7z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D7Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D7Z FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] </span></td></tr> | |
| - | [[Category: | + | <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=4d7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7z OCA], [http://pdbe.org/4d7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d7z RCSB], [http://www.ebi.ac.uk/pdbsum/4d7z PDBsum]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: Monteiro, D | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI]] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref> |
| - | [[Category: Webb, M | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspartate 1-decarboxylase]] | ||
| + | [[Category: Bravo, J P.K]] | ||
| + | [[Category: Monteiro, D C.F]] | ||
| + | [[Category: Pearson, A R]] | ||
| + | [[Category: Webb, M E]] | ||
| + | [[Category: Beta-alanine]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Pantothenate synthesis]] | ||
| + | [[Category: Protein derived cofactor]] | ||
| + | [[Category: Pyruvoyl cofactor]] | ||
Revision as of 20:18, 13 January 2016
E. coli L-aspartate-alpha-decarboxylase mutant N72Q to a resolution of 1.9 Angstroms
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