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5mt0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==COMPLEMENT FACTOR D IN COMPLEX WITH A REVERSIBLE INDOLE CARBOXYLIC ACID BASED INHIBITOR== | |
| + | <StructureSection load='5mt0' size='340' side='right'caption='[[5mt0]], [[Resolution|resolution]] 1.29Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mt0]] 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=5MT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MT0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.29Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QJS:5-FLUORANYL-3-[[(1~{S},2~{S})-2-PHENYLCYCLOPROPYL]CARBONYLAMINO]-1~{H}-INDOLE-2-CARBOXYLIC+ACID'>QJS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5mt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mt0 OCA], [https://pdbe.org/5mt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mt0 RCSB], [https://www.ebi.ac.uk/pdbsum/5mt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mt0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [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 == | ||
| + | [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. | ||
| - | + | ==See Also== | |
| - | + | *[[Complement C3 3D structures|Complement C3 3D structures]] | |
| - | + | *[[Complement factor 3D structures|Complement factor 3D structures]] | |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mac Sweeney A]] | ||
| + | [[Category: Ostermann N]] | ||
Current revision
COMPLEMENT FACTOR D IN COMPLEX WITH A REVERSIBLE INDOLE CARBOXYLIC ACID BASED INHIBITOR
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