5tca: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5tca is ~~ON HOLD until Paper Publication~~

==Complement Factor D inhibited with JH3==

~~Authors~~: ~~Stuckey~~, J.A.

== Structural highlights ==

<table><tr><td colspan='2'>[[5tca]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TCA OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TCA FirstGlance].

~~Description~~: ~~Complement~~ Factor D ~~inhibited~~ with ~~JH3~~

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=J55:1-(2-{(2S)-2-[(6-BROMOPYRIDIN-2-YL)CARBAMOYL]-1,3-THIAZOLIDIN-3-YL}-2-OXOETHYL)-1H-PYRAZOLO[3,4-B]PYRIDINE-3-CARBOXAMIDE'>J55</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5tcc|5tcc]]</td></tr>

[[Category: Stuckey, J.A]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tca OCA], [http://pdbe.org/5tca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tca RCSB], [http://www.ebi.ac.uk/pdbsum/5tca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tca ProSAT]</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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5tca is ON HOLD  until Paper Publication
+==Complement Factor D inhibited with JH3==
+<StructureSection load='5tca' size='340' side='right' caption='[[5tca]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
-Authors: Stuckey, J.A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5tca]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TCA FirstGlance]. <br>
-Description: Complement Factor D inhibited with JH3
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=J55:1-(2-{(2S)-2-[(6-BROMOPYRIDIN-2-YL)CARBAMOYL]-1,3-THIAZOLIDIN-3-YL}-2-OXOETHYL)-1H-PYRAZOLO[3,4-B]PYRIDINE-3-CARBOXAMIDE'>J55</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tcc|5tcc]]</td></tr>
-[[Category: Stuckey, J.A]]
+<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=5tca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tca OCA], [http://pdbe.org/5tca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tca RCSB], [http://www.ebi.ac.uk/pdbsum/5tca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tca 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]]