6x0h: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='6x0h' size='340' side='right'caption='[[6x0h]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6x0h]] 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=6X0H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X0H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6x0h]] 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=6X0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X0H 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=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.087&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sidA ([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=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0h OCA], [https://pdbe.org/6x0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x0h RCSB], [https://www.ebi.ac.uk/pdbsum/6x0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0h 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=6x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0h OCA], [http://pdbe.org/6x0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x0h RCSB], [http://www.ebi.ac.uk/pdbsum/6x0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0h ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Aspfu]]
+[[Category: Aspergillus fumigatus Af293]]
 [[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]]