5mhm

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Current revision (12:46, 26 July 2023) (edit) (undo)
 
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<StructureSection load='5mhm' size='340' side='right'caption='[[5mhm]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
<StructureSection load='5mhm' size='340' side='right'caption='[[5mhm]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mhm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MHM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MHM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mhm]] 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=5MHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MHM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1TX:(2S)-2-AMINO-7-METHOXY-7-OXOHEPTANOIC+ACID'>1TX</scene>, <scene name='pdbligand=7NW:'>7NW</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></td></tr>
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<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=7NW:2-methyl-1,3-thiazole-4-carboxylic+acid'>7NW</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kty|4kty]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mhm OCA], [https://pdbe.org/5mhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mhm RCSB], [https://www.ebi.ac.uk/pdbsum/5mhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mhm ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mhm OCA], [http://pdbe.org/5mhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mhm RCSB], [http://www.ebi.ac.uk/pdbsum/5mhm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mhm ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/F13A_HUMAN F13A_HUMAN]] Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:[http://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>
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[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 ==
== Function ==
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[[http://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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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On active duty: The available drugs for cardiovascular diseases can promote blood clotting but can also lead to life-threatening bleeding episodes. A promising target for the development of safer alternatives is the transglutaminase Factor XIII (FXIII), the active structure of which is presented. The binding and coordination of three calcium ions induce major domain movements in the enzyme upon activation.
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Structure of Active Coagulation Factor XIII Triggered by Calcium Binding: Basis for the Design of Next-Generation Anticoagulants.,Stieler M, Weber J, Hils M, Kolb P, Heine A, Buchold C, Pasternack R, Klebe G Angew Chem Int Ed Engl. 2013 Sep 20. doi: 10.1002/anie.201305133. PMID:24115223<ref>PMID:24115223</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5mhm" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-glutamine gamma-glutamyltransferase]]
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[[Category: Synthetic construct]]
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[[Category: Heine, A]]
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[[Category: Heine A]]
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[[Category: Klebe, G]]
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[[Category: Klebe G]]
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[[Category: Stieler, M]]
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[[Category: Stieler M]]
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[[Category: Factor xiii]]
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[[Category: Hydrolase]]
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[[Category: Inhibition]]
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[[Category: Transglutaminase]]
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Current revision

FXIIIa in complex with the inhibitor ZED1630

PDB ID 5mhm

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