5tcc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Complement Factor D inhibited with JH4== | |
| - | + | <StructureSection load='5tcc' size='340' side='right' caption='[[5tcc]], [[Resolution|resolution]] 3.37Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5tcc]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TCC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=J56:(2S)-N-(6-BROMOPYRIDIN-2-YL)-3-[(1H-INDAZOL-1-YL)ACETYL]-1,3-THIAZOLIDINE-2-CARBOXAMIDE'>J56</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tca|5tca]]</td></tr> |
| - | [[Category: Stuckey, J | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tcc OCA], [http://pdbe.org/5tcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tcc RCSB], [http://www.ebi.ac.uk/pdbsum/5tcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tcc 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: Stuckey, J A]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Serine protease]] | ||
Revision as of 01:03, 20 October 2016
Complement Factor D inhibited with JH4
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