2h5c: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2H5C is a | 2H5C is a 1 chain 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=2H5C 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: Agard, D A.]] | [[Category: Agard, D A.]] | ||
[[Category: Daugherty, M D.]] | [[Category: Daugherty, M D.]] | ||
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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 Mon Feb 16 17:59:29 2009'' |
Revision as of 18:59, 16 February 2009
0.82A resolution crystal structure of alpha-lytic protease at pH 50.82A resolution crystal structure of alpha-lytic protease at pH 5
Template:ABSTRACT PUBMED 16834383
About this StructureAbout this Structure
2H5C is a 1 chain structure of sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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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