6fuh: Difference between revisions

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==Complement factor D in complex with the inhibitor (4-((3-(aminomethyl)phenyl)amino)quinazolin-2-yl)-L-valine==
==Complement factor D in complex with the inhibitor (4-((3-(aminomethyl)phenyl)amino)quinazolin-2-yl)-L-valine==
<StructureSection load='6fuh' size='340' side='right' caption='[[6fuh]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
<StructureSection load='6fuh' size='340' side='right'caption='[[6fuh]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6fuh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUH FirstGlance]. <br>
<table><tr><td colspan='2'>[[6fuh]] 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=6FUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FUH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E88:(2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]-3-methyl-butanoic+acid'>E88</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]] 1.37&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fug|6fug]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E88:(2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]-3-methyl-butanoic+acid'>E88</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuh OCA], [https://pdbe.org/6fuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fuh RCSB], [https://www.ebi.ac.uk/pdbsum/6fuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuh ProSAT]</span></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=6fuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuh OCA], [http://pdbe.org/6fuh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fuh RCSB], [http://www.ebi.ac.uk/pdbsum/6fuh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuh ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== 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 ==
== 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.
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6fuh" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6fuh" style="background-color:#fffaf0;"></div>
==See Also==
*[[Complement factor 3D structures|Complement factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</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]]

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