3guz
From Proteopedia
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===Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's=== | ===Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3guz]] 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=3GUZ OCA]. | |
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| + | ==See Also== | ||
| + | *[[Pantothenate synthetase|Pantothenate synthetase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020059543</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Pantoate--beta-alanine ligase]] | [[Category: Pantoate--beta-alanine ligase]] | ||
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[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Competitive inhibition]] | [[Category: Competitive inhibition]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
[[Category: Non-canonical pantoate binding-site]] | [[Category: Non-canonical pantoate binding-site]] | ||
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[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
[[Category: Substrate binding]] | [[Category: Substrate binding]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 17:22:51 2010'' | ||
Revision as of 15:40, 27 February 2013
Contents |
Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's
Template:ABSTRACT PUBMED 20059543
About this Structure
3guz is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Chakrabarti KS, Thakur KG, Gopal B, Sarma SP. X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate. FEBS J. 2010 Feb;277(3):697-712. Epub 2010 Jan 4. PMID:20059543 doi:10.1111/j.1742-4658.2009.07515.x
