4ec3
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ec3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eschscholzia_californica Eschscholzia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EC3 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=REN:(S)-RETICULINE'>REN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d2j|3d2j]], [[3d2d|3d2d]], [[3fw7|3fw7]], [[3fw8|3fw8]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d2j|3d2j]], [[3d2d|3d2d]], [[3fw7|3fw7]], [[3fw8|3fw8]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 Eschscholzia californica])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBE, BBE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3467 Eschscholzia californica])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Reticuline_oxidase Reticuline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.3 1.21.3.3] </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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 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=4ec3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ec3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ec3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ec3 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RETO_ESCCA RETO_ESCCA]] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Eschscholzia californica]] | [[Category: Eschscholzia californica]] | ||
[[Category: Reticuline oxidase]] | [[Category: Reticuline oxidase]] | ||
| - | [[Category: Gruber, K | + | [[Category: Gruber, K]] |
| - | [[Category: Macheroux, P | + | [[Category: Macheroux, P]] |
| - | [[Category: Winkler, A | + | [[Category: Winkler, A]] |
[[Category: Bi-covalent flavinylation]] | [[Category: Bi-covalent flavinylation]] | ||
[[Category: Fad]] | [[Category: Fad]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: P-cresol methyl hydroxylase superfamily]] | [[Category: P-cresol methyl hydroxylase superfamily]] | ||
Revision as of 04:25, 25 December 2014
Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline
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