2h5d

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==About this Structure==
==About this Structure==
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2H5D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5D OCA].
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2H5D is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5D OCA].
==Reference==
==Reference==
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Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16834383 16834383]
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<ref group="xtra">PMID:16834383</ref><references group="xtra"/>
[[Category: Alpha-lytic endopeptidase]]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
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[[Category: Single protein]]
 
[[Category: Agard, D A.]]
[[Category: Agard, D A.]]
[[Category: Fuhrmann, C N.]]
[[Category: Fuhrmann, C N.]]
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[[Category: Ultra-high resolution]]
[[Category: Ultra-high resolution]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:41:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:18:52 2009''

Revision as of 12:18, 17 February 2009

Template:STRUCTURE 2h5d

0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid

Template:ABSTRACT PUBMED 16834383

About this Structure

2H5D is a 2 chains structure of sequences from Lysobacter enzymogenes. Full crystallographic information is available from OCA.

Reference

  • Fuhrmann CN, Daugherty MD, Agard DA. Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis. J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:16834383 doi:http://dx.doi.org/10.1021/ja057721o

Page seeded by OCA on Tue Feb 17 14:18:52 2009

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