2jkh

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m (Protected "2jkh" [edit=sysop:move=sysop])
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[[Image:2jkh.png|left|200px]]
[[Image:2jkh.png|left|200px]]
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{{STRUCTURE_2jkh| PDB=2jkh | SCENE= }}
{{STRUCTURE_2jkh| PDB=2jkh | SCENE= }}
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==About this Structure==
==About this Structure==
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[[2jkh]] is a 2 chain structure with 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=2JKH OCA].
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[[2jkh]] is a 2 chain structure of [[Factor Xa]] with 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=2JKH OCA].
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==See Also==
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*[[Factor Xa|Factor Xa]]
==Reference==
==Reference==
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<ref group="xtra">PMID:19101972</ref><references group="xtra"/>
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<ref group="xtra">PMID:019101972</ref><references group="xtra"/>
[[Category: Coagulation factor Xa]]
[[Category: Coagulation factor Xa]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Schweizer, W B.]]
[[Category: Schweizer, W B.]]
[[Category: Seiler, P.]]
[[Category: Seiler, P.]]
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[[Category: Blood coagulation]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Coagulation factor]]
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[[Category: Egf-like domain]]
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[[Category: Gamma-carboxyglutamic acid]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Hydroxylation]]
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[[Category: Plasma]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Serine protease]]
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[[Category: Zymogen]]

Revision as of 23:01, 26 July 2012

Template:STRUCTURE 2jkh

Contents

FACTOR XA - CATION INHIBITOR COMPLEX

About this Structure

2jkh is a 2 chain structure of Factor Xa with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Salonen LM, Bucher C, Banner DW, Haap W, Mary JL, Benz J, Kuster O, Seiler P, Schweizer WB, Diederich F. Cation-pi interactions at the active site of factor Xa: dramatic enhancement upon stepwise N-alkylation of ammonium ions. Angew Chem Int Ed Engl. 2009;48(4):811-4. PMID:19101972 doi:10.1002/anie.200804695

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