3h1x

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[[Image:3h1x.png|left|200px]]
[[Image:3h1x.png|left|200px]]
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{{STRUCTURE_3h1x| PDB=3h1x | SCENE= }}
{{STRUCTURE_3h1x| PDB=3h1x | SCENE= }}
===Simultaneous inhibition of anti-coagulation and inflammation: Crystal structure of phospholipase A2 complexed with indomethacin at 1.4 A resolution reveals the presence of the new common ligand binding site===
===Simultaneous inhibition of anti-coagulation and inflammation: Crystal structure of phospholipase A2 complexed with indomethacin at 1.4 A resolution reveals the presence of the new common ligand binding site===
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{{ABSTRACT_PUBMED_19462410}}
{{ABSTRACT_PUBMED_19462410}}
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==See Also==
==See Also==
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*[[Phospholipase A2]]
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*[[Phospholipase A2|Phospholipase A2]]
==Reference==
==Reference==
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<ref group="xtra">PMID:19462410</ref><references group="xtra"/>
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<ref group="xtra">PMID:019462410</ref><references group="xtra"/>
[[Category: Daboia russellii russellii]]
[[Category: Daboia russellii russellii]]
[[Category: Kaur, P.]]
[[Category: Kaur, P.]]
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[[Category: Anti-coagulant]]
[[Category: Anti-coagulant]]
[[Category: Anti-inflammatory]]
[[Category: Anti-inflammatory]]
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[[Category: Crystal structure]]
 
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Indomethacin]]
[[Category: Indomethacin]]
[[Category: Pla2]]
[[Category: Pla2]]

Revision as of 06:46, 27 July 2012

Template:STRUCTURE 3h1x

Contents

Simultaneous inhibition of anti-coagulation and inflammation: Crystal structure of phospholipase A2 complexed with indomethacin at 1.4 A resolution reveals the presence of the new common ligand binding site

Template:ABSTRACT PUBMED 19462410

About this Structure

3h1x is a 1 chain structure of Phospholipase A2 with sequence from Daboia russellii russellii. Full crystallographic information is available from OCA.

See Also

Reference

  • Singh N, Kumar RP, Kumar S, Sharma S, Mir R, Kaur P, Srinivasan A, Singh TP. Simultaneous inhibition of anti-coagulation and inflammation: crystal structure of phospholipase A(2) complexed with indomethacin at 1.4 A resolution reveals the presence of the new common ligand-binding site. J Mol Recognit. 2009 May 21. PMID:19462410 doi:10.1002/jmr.960

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