2f91

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==About this Structure==
==About this Structure==
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2F91 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Pontastacus_leptodactylus Pontastacus leptodactylus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yr4 1yr4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F91 OCA].
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[[2f91]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pontastacus_leptodactylus Pontastacus leptodactylus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yr4 1yr4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F91 OCA].
==Reference==
==Reference==
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[[Category: Atomic resolution]]
[[Category: Atomic resolution]]
[[Category: Canonical inhibitor]]
[[Category: Canonical inhibitor]]
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[[Category: Hydrolase/hydrolase inhibitor complex]]
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Trypsin]]
[[Category: Trypsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:58:36 2009''
 

Revision as of 23:44, 14 March 2011

Template:STRUCTURE 2f91

1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI

Template:ABSTRACT PUBMED 16475800

About this Structure

2f91 is a 2 chain structure with sequence from Pontastacus leptodactylus. This structure supersedes the now removed PDB entry 1yr4. Full crystallographic information is available from OCA.

Reference

  • Fodor K, Harmat V, Neutze R, Szilagyi L, Graf L, Katona G. Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis. Biochemistry. 2006 Feb 21;45(7):2114-21. PMID:16475800 doi:10.1021/bi0517133
  • Fodor K, Harmat V, Hetenyi C, Kardos J, Antal J, Perczel A, Patthy A, Katona G, Graf L. Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition. J Mol Biol. 2005 Jul 1;350(1):156-69. PMID:15922357 doi:10.1016/j.jmb.2005.04.039

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