2oa1
From Proteopedia
(Difference between revisions)
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<StructureSection load='2oa1' size='340' side='right'caption='[[2oa1]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='2oa1' size='340' side='right'caption='[[2oa1]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2oa1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2oa1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OA1 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oa1 OCA], [https://pdbe.org/2oa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oa1 RCSB], [https://www.ebi.ac.uk/pdbsum/2oa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oa1 ProSAT]</span></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=2oa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oa1 OCA], [https://pdbe.org/2oa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oa1 RCSB], [https://www.ebi.ac.uk/pdbsum/2oa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oa1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/REBH_LENAE REBH_LENAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp.<ref>PMID:11983340</ref> <ref>PMID:15743914</ref> <ref>PMID:17260957</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Lentzea aerocolonigenes]] |
- | [[Category: | + | [[Category: Bingman CA]] |
- | [[Category: | + | [[Category: Bitto E]] |
- | [[Category: | + | [[Category: Phillips Jr GN]] |
- | [[Category: | + | [[Category: Singh S]] |
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Current revision
Crystal Structure of RebH, a FAD-dependent halogenase from Lechevalieria aerocolonigenes, the L-Tryptophan with FAD complex
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