3gds
From Proteopedia
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{{STRUCTURE_3gds| PDB=3gds | SCENE= }} | {{STRUCTURE_3gds| PDB=3gds | SCENE= }} | ||
===Crystal structure of DegS H198P/D320A mutant modified by DFP in complex with DNRDGNVYYF peptide=== | ===Crystal structure of DegS H198P/D320A mutant modified by DFP in complex with DNRDGNVYYF peptide=== | ||
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{{ABSTRACT_PUBMED_19836340}} | {{ABSTRACT_PUBMED_19836340}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3gds]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GDS OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019836340</ref><references group="xtra"/> |
| - | [[Category: Escherichia coli | + | [[Category: Escherichia coli]] |
[[Category: Grant, R A.]] | [[Category: Grant, R A.]] | ||
[[Category: Sauer, R T.]] | [[Category: Sauer, R T.]] | ||
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[[Category: Htra]] | [[Category: Htra]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
| - | [[Category: Hydrolase | + | [[Category: Hydrolase-hydrolase activator complex]] |
[[Category: Pdz omp]] | [[Category: Pdz omp]] | ||
| - | [[Category: Periplasm]] | ||
[[Category: Protease]] | [[Category: Protease]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
[[Category: Stress-sensor]] | [[Category: Stress-sensor]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 09:01:51 2010'' | ||
Revision as of 14:23, 20 February 2013
Crystal structure of DegS H198P/D320A mutant modified by DFP in complex with DNRDGNVYYF peptide
Template:ABSTRACT PUBMED 19836340
About this Structure
3gds is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Sohn J, Grant RA, Sauer RT. OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure. 2009 Oct 14;17(10):1411-21. PMID:19836340 doi:10.1016/j.str.2009.07.017
