5mho: Difference between revisions

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

~~The~~ entry ~~5mho~~ is ~~ON HOLD~~

==FXIIIa in complex with the inhibitor ZED2369==

== Structural highlights ==

<table><tr><td colspan='2'>[[5mho]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MHO OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=5MHO FirstGlance].

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.92Å</td></tr>

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1TX:(2S)-2-AMINO-7-METHOXY-7-OXOHEPTANOIC+ACID'>1TX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRM:1H-BENOXIMIDAZOLE-2-CARBOXYLIC+ACID'>TRM</scene></td></tr>

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

</table>

== Disease ==

[https://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN] Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:[https://omim.org/entry/613225 613225]. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.<ref>PMID:1353995</ref>

== Function ==

[https://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN] Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.

~~Authors~~:

==See Also==

*[[Factor XIII|Factor XIII]]

~~Description~~:

== References ==

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

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Synthetic construct]]

[[Category: Heine A]]

[[Category: Klebe G]]

[[Category: Stieler M]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5mho is ON HOLD
+==FXIIIa in complex with the inhibitor ZED2369==
+<StructureSection load='5mho' size='340' side='right'caption='[[5mho]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5mho]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MHO 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]] 2.92&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1TX:(2S)-2-AMINO-7-METHOXY-7-OXOHEPTANOIC+ACID'>1TX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRM:1H-BENOXIMIDAZOLE-2-CARBOXYLIC+ACID'>TRM</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=5mho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mho OCA], [https://pdbe.org/5mho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mho RCSB], [https://www.ebi.ac.uk/pdbsum/5mho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mho ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN] Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:[https://omim.org/entry/613225 613225]. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.<ref>PMID:1353995</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN] Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
-Authors:
+==See Also==
+*[[Factor XIII|Factor XIII]]
-Description:
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Heine A]]
+[[Category: Klebe G]]
+[[Category: Stieler M]]