2h5d
From Proteopedia
(Difference between revisions)
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==About this Structure== | ==About this Structure== | ||
- | 2H5D is a | + | 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== | ||
- | + | <ref group="xtra">PMID:16834383</ref><references group="xtra"/> | |
[[Category: Alpha-lytic endopeptidase]] | [[Category: Alpha-lytic endopeptidase]] | ||
[[Category: Lysobacter enzymogenes]] | [[Category: Lysobacter enzymogenes]] | ||
- | [[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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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
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