5fck

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==COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5==
==COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5==
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<StructureSection load='5fck' size='340' side='right' caption='[[5fck]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='5fck' size='340' side='right'caption='[[5fck]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fck]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FCK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fck]] 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=5FCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FCK 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=5WC:1-[2-[(1~{R},3~{S},5~{R})-3-[[(1~{R})-1-(3-CHLORANYL-2-FLUORANYL-PHENYL)ETHYL]CARBAMOYL]-2-AZABICYCLO[3.1.0]HEXAN-2-YL]-2-OXIDANYLIDENE-ETHYL]PYRAZOLO[3,4-C]PYRIDINE-3-CARBOXAMIDE'>5WC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.86&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5WC:1-[2-[(1~{R},3~{S},5~{R})-3-[[(1~{R})-1-(3-CHLORANYL-2-FLUORANYL-PHENYL)ETHYL]CARBAMOYL]-2-AZABICYCLO[3.1.0]HEXAN-2-YL]-2-OXIDANYLIDENE-ETHYL]PYRAZOLO[3,4-C]PYRIDINE-3-CARBOXAMIDE'>5WC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5fck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fck OCA], [http://pdbe.org/5fck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fck RCSB], [http://www.ebi.ac.uk/pdbsum/5fck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fck ProSAT]</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=5fck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fck OCA], [https://pdbe.org/5fck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fck RCSB], [https://www.ebi.ac.uk/pdbsum/5fck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fck ProSAT]</span></td></tr>
</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 5fck" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5fck" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Complement C3 3D structures|Complement C3 3D structures]]
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*[[Complement factor 3D structures|Complement factor 3D structures]]
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 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: Sweeney, A Mac]]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Mac Sweeney A]]

Current revision

COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5

PDB ID 5fck

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