4b64: Difference between revisions
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<StructureSection load='4b64' size='340' side='right'caption='[[4b64]], [[Resolution|resolution]] 2.28Å' scene=''> | <StructureSection load='4b64' size='340' side='right'caption='[[4b64]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b64]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4b64]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B64 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b63|4b63]], [[4b65|4b65]], [[4b67|4b67]], [[4b68|4b68]], [[4b69|4b69]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b63|4b63]], [[4b65|4b65]], [[4b67|4b67]], [[4b68|4b68]], [[4b69|4b69]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b64 OCA], [https://pdbe.org/4b64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b64 RCSB], [https://www.ebi.ac.uk/pdbsum/4b64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b64 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Monooxygenase|Monooxygenase]] | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 10:01, 31 August 2022
A. fumigatus ornithine hydroxylase (SidA) bound to NADP and LysineA. fumigatus ornithine hydroxylase (SidA) bound to NADP and Lysine
Structural highlights
Publication Abstract from PubMedSidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N(5)-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP(+), and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes. Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases.,Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A Biochemistry. 2012 Sep 11;51(36):7043-5. Epub 2012 Aug 30. PMID:22928747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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