6fui: Difference between revisions

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 ==Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol==
-<StructureSection load='6fui' size='340' side='right' caption='[[6fui]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
+<StructureSection load='6fui' size='340' side='right'caption='[[6fui]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6fui]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6fui]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FUI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E7W:(1~{R},2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]cyclohexane-1-carboxylic+acid'>E7W</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]] 1.38&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Complement_factor_D Complement factor D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E7W:(1~{R},2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]cyclohexane-1-carboxylic+acid'>E7W</scene></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=6fui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fui OCA], [http://pdbe.org/6fui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fui RCSB], [http://www.ebi.ac.uk/pdbsum/6fui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fui 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=6fui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fui OCA], [https://pdbe.org/6fui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fui RCSB], [https://www.ebi.ac.uk/pdbsum/6fui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fui ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN]] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[http://omim.org/entry/613912 613912]]. CFDD is an immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.
+[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[https://omim.org/entry/613912 613912]. CFDD is an immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.
 == Function ==
-[[http://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN]] Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
+[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 </div>
 <div class="pdbe-citations 6fui" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Complement factor 3D structures|Complement factor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Complement factor D]]
+[[Category: Homo sapiens]]
-[[Category: Erbel, P]]
+[[Category: Large Structures]]
-[[Category: Lorthiois, E]]
+[[Category: Erbel P]]
-[[Category: Maibaum, J]]
+[[Category: Lorthiois E]]
-[[Category: Ostermann, N]]
+[[Category: Mac Sweeney A]]
-[[Category: Randl, S]]
+[[Category: Maibaum J]]
-[[Category: Ruedisser, S]]
+[[Category: Ostermann N]]
-[[Category: Sweeney, A Mac]]
+[[Category: Randl S]]
-[[Category: Vulpetti, A]]
+[[Category: Ruedisser S]]
-[[Category: Yoon, T]]
+[[Category: Vulpetti A]]
-[[Category: Complex]]
+[[Category: Yoon T]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]
-[[Category: Serine protease]]