Ecotin: Difference between revisions

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<StructureSection load='1id5' size='400' side='right' scene='' caption='A monomer of the dimeric E. coli ecotin (gold) complex with thrombin heavy chain (pink) and light chain (aqua), protease inhibitor and Ca+2 ion (green) [[1id5]]'>
<StructureSection load='1id5' size='400' side='right' scene='46/465444/Cv/2' caption='The dimeric E. coli ecotin (yellow) complex with thrombin heavy chain (cyan) and light chain (magenta) and Ca+2 ion (green) [[1id5]]'>


'''Ecotin''' (ECO) is a serine protease inhibitor found in the periplasm of ''E. coli''.  It is a potent anti and a reversible tight-binding inhibitor of human factor Xa.<ref>PMID:14705961</ref>
'''Ecotin''' (ECO) is a serine protease inhibitor found in the periplasm of ''E. coli''.  It is a potent anti and a reversible tight-binding inhibitor of human factor Xa.<ref>PMID:14705961</ref>
<scene name='46/465444/Cv/7'>The dimeric E. coli ecotin</scene> with <scene name='46/465444/Cv/8'>thrombin heavy and light chains</scene>.
<scene name='46/465444/Cv/9'>Ca+2 ion coordination site</scene> in thrombin heavy chain ([[1id5]]).<ref>PMID:11513582</ref> Water molecules shown as red spheres.
</StructureSection>
</StructureSection>
== 3D Structures of Ecotin ==
== 3D Structures of Ecotin ==
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**[[1fi8]] - ECO (mutant) + granzyme B<br />
**[[1fi8]] - ECO (mutant) + granzyme B<br />
**[[4iw4]] – ECO + mannan-binding lectin serine protease<br />
**[[4iw4]] – ECO + mannan-binding lectin serine protease<br />
**[[7cbk]] – ECO + elastase<br />
**[[7pqo]] – ECO (mutant) + MASP-1<br />
**[[7pqn]] – ECO + MASP-2<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 09:53, 8 February 2023

The dimeric E. coli ecotin (yellow) complex with thrombin heavy chain (cyan) and light chain (magenta) and Ca+2 ion (green) 1id5

Drag the structure with the mouse to rotate

3D Structures of Ecotin

Updated on 08-February-2023

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky