4bab
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4bab is ON HOLD Authors: Bartsch, S., Wybenga, G.G., Jansen, M., Heberling, M.M., Wu, B., Dijkstra, B.W., Janssen, D.B. Description: Redesign of a ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Redesign of a Phenylalanine Aminomutase into a beta-Phenylalanine Ammonia Lyase== | |
| + | <StructureSection load='4bab' size='340' side='right'caption='[[4bab]], [[Resolution|resolution]] 2.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bab]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Taxus_chinensis Taxus chinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BAB FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bab OCA], [https://pdbe.org/4bab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bab RCSB], [https://www.ebi.ac.uk/pdbsum/4bab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bab ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PAM_TAXCH PAM_TAXCH] Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.<ref>PMID:15878763</ref> <ref>PMID:22113970</ref> <ref>PMID:24786474</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Aminomutase 3D structures|Aminomutase 3D structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Taxus chinensis]] | ||
| + | [[Category: Bartsch S]] | ||
| + | [[Category: Dijkstra BW]] | ||
| + | [[Category: Heberling MM]] | ||
| + | [[Category: Jansen M]] | ||
| + | [[Category: Janssen DB]] | ||
| + | [[Category: Wu B]] | ||
| + | [[Category: Wybenga GG]] | ||
Current revision
Redesign of a Phenylalanine Aminomutase into a beta-Phenylalanine Ammonia Lyase
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