2h5c
From Proteopedia
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[[Image:2h5c.png|left|200px]] | [[Image:2h5c.png|left|200px]] | ||
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{{STRUCTURE_2h5c| PDB=2h5c | SCENE= }} | {{STRUCTURE_2h5c| PDB=2h5c | SCENE= }} | ||
===0.82A resolution crystal structure of alpha-lytic protease at pH 5=== | ===0.82A resolution crystal structure of alpha-lytic protease at pH 5=== | ||
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{{ABSTRACT_PUBMED_16834383}} | {{ABSTRACT_PUBMED_16834383}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2h5c]] is a 1 chain structure with 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: | + | <ref group="xtra">PMID:016834383</ref><references group="xtra"/> |
[[Category: Alpha-lytic endopeptidase]] | [[Category: Alpha-lytic endopeptidase]] | ||
[[Category: Lysobacter enzymogenes]] | [[Category: Lysobacter enzymogenes]] | ||
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[[Category: Acylation transition state]] | [[Category: Acylation transition state]] | ||
[[Category: Catalysis]] | [[Category: Catalysis]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Packing distortion]] | [[Category: Packing distortion]] | ||
[[Category: Protein folding]] | [[Category: Protein folding]] | ||
[[Category: Protein stability]] | [[Category: Protein stability]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
| - | [[Category: Ultra-high resolution]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:59:29 2009'' | ||
Revision as of 12:50, 7 January 2013
0.82A resolution crystal structure of alpha-lytic protease at pH 5
Template:ABSTRACT PUBMED 16834383
About this Structure
2h5c is a 1 chain structure with sequence 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
