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<StructureSection load='7jvl' size='340' side='right'caption='[[7jvl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='7jvl' size='340' side='right'caption='[[7jvl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7jvl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JVL FirstGlance]. <br>
<table><tr><td colspan='2'>[[7jvl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JVL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sidA, Afu2g07680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-ornithine_N(5)-monooxygenase_(NAD(P)H) L-ornithine N(5)-monooxygenase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.196 1.14.13.196] </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=7jvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvl OCA], [https://pdbe.org/7jvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jvl RCSB], [https://www.ebi.ac.uk/pdbsum/7jvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvl ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvl OCA], [http://pdbe.org/7jvl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jvl RCSB], [http://www.ebi.ac.uk/pdbsum/7jvl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SIDA_ASPFU SIDA_ASPFU]] Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC). Highly specific for its substrate, only hydrolyzing l-ornithine. Has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate. Essential for virulence.<ref>PMID:15504822</ref> <ref>PMID:16113265</ref> <ref>PMID:20614882</ref> <ref>PMID:22465572</ref>
[https://www.uniprot.org/uniprot/SIDA_ASPFU SIDA_ASPFU] Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC). Highly specific for its substrate, only hydrolyzing l-ornithine. Has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate. Essential for virulence.<ref>PMID:15504822</ref> <ref>PMID:16113265</ref> <ref>PMID:20614882</ref> <ref>PMID:22465572</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 7jvl" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7jvl" style="background-color:#fffaf0;"></div>
==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspfu]]
[[Category: Aspergillus fumigatus Af293]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Campbell, A C]]
[[Category: Campbell AC]]
[[Category: Tanner, J J]]
[[Category: Tanner JJ]]
[[Category: Flavin-containing monooxygenase]]
[[Category: Flavoprotein]]
[[Category: Oxidoreductase]]
Retrieved from "https://proteopedia.org/7jvl"