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[[Image:1evu.jpg|left|200px]]


{{Structure
==HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE==
|PDB= 1evu |SIZE=350|CAPTION= <scene name='initialview01'>1evu</scene>, resolution 2.01&Aring;
<StructureSection load='1evu' size='340' side='right'caption='[[1evu]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=PGO:1,2-PROPANEDIOL'>PGO</scene>
<table><tr><td colspan='2'>[[1evu]] is a 2 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=1EVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EVU FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
|GENE=  
<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=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</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=1evu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evu OCA], [https://pdbe.org/1evu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1evu RCSB], [https://www.ebi.ac.uk/pdbsum/1evu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1evu 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/1evu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1evu ConSurf].
<div style="clear:both"></div>


'''HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE'''
==See Also==
 
*[[Factor XIII|Factor XIII]]
 
== References ==
==Disease==
<references/>
Known disease associated with this structure: Factor XIIIA deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134570 134570]]
__TOC__
 
</StructureSection>
==About this Structure==
1EVU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVU OCA].
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bishop PD]]
[[Category: Bishop, P D.]]
[[Category: Garzon RJ]]
[[Category: Garzon, R J.]]
[[Category: Le Trong I]]
[[Category: Pratt, K P.]]
[[Category: Pratt KP]]
[[Category: Stenkamp, R E.]]
[[Category: Stenkamp RE]]
[[Category: Teller, D C.]]
[[Category: Teller DC]]
[[Category: Trong, I Le.]]
[[Category: CA]]
[[Category: PGO]]
[[Category: blood coagulation]]
[[Category: calcium]]
[[Category: transglutaminase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:57 2008''

Latest revision as of 13:07, 20 March 2024

HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITEHUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE

Structural highlights

1evu is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.01Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

F13A_HUMAN Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [MIM:613225. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.[1]

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Board P, Coggan M, Miloszewski K. Identification of a point mutation in factor XIII A subunit deficiency. Blood. 1992 Aug 15;80(4):937-41. PMID:1353995

1evu, resolution 2.01Å

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