2xw9

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==Crystal Structure of Complement Factor D mutant S183A==
==Crystal Structure of Complement Factor D mutant S183A==
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<StructureSection load='2xw9' size='340' side='right' caption='[[2xw9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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<StructureSection load='2xw9' size='340' side='right'caption='[[2xw9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xw9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XW9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xw9]] 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=2XW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XW9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dst|1dst]], [[1dfp|1dfp]], [[1dic|1dic]], [[2xwa|2xwa]], [[1bio|1bio]], [[2xwb|2xwb]], [[1dsu|1dsu]], [[1hfd|1hfd]], [[1fdp|1fdp]], [[2xwj|2xwj]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw9 OCA], [https://pdbe.org/2xw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xw9 RCSB], [https://www.ebi.ac.uk/pdbsum/2xw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xw9 ProSAT]</span></td></tr>
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<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=2xw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw9 OCA], [http://pdbe.org/2xw9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xw9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xw9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xw9 ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[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.
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[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 ==
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[[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.
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 2xw9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2xw9" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Complement factor 3D structures|Complement factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Complement factor D]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Forneris, F]]
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[[Category: Forneris F]]
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[[Category: Gros, P]]
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[[Category: Gros P]]
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[[Category: Lambris, J D]]
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[[Category: Lambris JD]]
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[[Category: Ricklin, D]]
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[[Category: Ricklin D]]
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[[Category: Tzekou, A]]
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[[Category: Tzekou A]]
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[[Category: Wallace, R S]]
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[[Category: Wallace RS]]
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[[Category: Wu, J]]
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[[Category: Wu J]]
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[[Category: Alternative pathway]]
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[[Category: Hydrolase]]
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[[Category: Immune system]]
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[[Category: Serine protease]]
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Current revision

Crystal Structure of Complement Factor D mutant S183A

PDB ID 2xw9

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