5fck
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5== | |
| - | + | <StructureSection load='5fck' size='340' side='right' caption='[[5fck]], [[Resolution|resolution]] 1.86Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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> | |
| - | + | </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> | |
| - | [[Category: | + | <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> |
| - | [[Category: | + | <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> |
| + | </table> | ||
| + | == 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. | ||
| + | == 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Complement factor D]] | ||
| + | [[Category: Sweeney, A Mac]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 18:40, 26 October 2016
COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5
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