2xwa

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Current revision (10:40, 20 December 2023) (edit) (undo)
 
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<StructureSection load='2xwa' size='340' side='right'caption='[[2xwa]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='2xwa' size='340' side='right'caption='[[2xwa]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xwa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XWA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xwa]] is a 2 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=2XWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XWA FirstGlance]. <br>
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</td></tr><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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dfp|1dfp]], [[1dic|1dic]], [[1dst|1dst]], [[2xw9|2xw9]], [[1bio|1bio]], [[2xwb|2xwb]], [[1dsu|1dsu]], [[1hfd|1hfd]], [[1fdp|1fdp]], [[2xwj|2xwj]]</div></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'>[https://en.wikipedia.org/wiki/Complement_factor_D Complement factor D], with EC number [https://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=2xwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwa OCA], [https://pdbe.org/2xwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xwa RCSB], [https://www.ebi.ac.uk/pdbsum/2xwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xwa 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=2xwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwa OCA], [https://pdbe.org/2xwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xwa RCSB], [https://www.ebi.ac.uk/pdbsum/2xwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xwa ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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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.
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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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[[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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[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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__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]]
[[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 R202A

PDB ID 2xwa

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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