This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5mhn
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5mhn is ON HOLD Authors: Description: Category: Unreleased Structures) |
|||
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==FXIIIa in complex with the inhibitor ZED2360== | |
| + | <StructureSection load='5mhn' size='340' side='right'caption='[[5mhn]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mhn]] 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=5MHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MHN 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]] 2.48Å</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=7NF:2-ethoxycarbonyl-1,3-thiazole-4-carboxylic+acid'>7NF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5mhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mhn OCA], [https://pdbe.org/5mhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mhn RCSB], [https://www.ebi.ac.uk/pdbsum/5mhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mhn 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Factor XIII|Factor XIII]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Heine A]] | ||
| + | [[Category: Klebe G]] | ||
| + | [[Category: Stieler M]] | ||
Current revision
FXIIIa in complex with the inhibitor ZED2360
| |||||||||||
