5fck: Difference between revisions

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<StructureSection load='5fck' size='340' side='right'caption='[[5fck]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
<StructureSection load='5fck' size='340' side='right'caption='[[5fck]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5fck]] 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=5FCK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FCK FirstGlance]. <br>
<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>
</td></tr><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>
</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CFD, DF, PFD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<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>
<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=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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
</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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Complement factor D]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sweeney, A Mac]]
[[Category: Mac Sweeney A]]
[[Category: Hydrolase]]

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