3e2q: Difference between revisions

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New page: '''Unreleased structure''' The entry 3e2q is ON HOLD Authors: Tanner, J.J. Description: Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with trans-4-hydroxy-L-proline ''Pa...
 
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'''Unreleased structure'''
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[[Image:3e2q.jpg|left|200px]]


The entry 3e2q is ON HOLD
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Authors: Tanner, J.J.
===Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with trans-4-hydroxy-L-proline===


Description: Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with trans-4-hydroxy-L-proline


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 13 13:44:19 2008''
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{{ABSTRACT_PUBMED_19140736}}
 
==About this Structure==
3E2Q is a 1 chain structure of 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=3E2Q OCA].
 
==Reference==
<ref group="xtra">PMID:19140736</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Proline dehydrogenase]]
[[Category: Tanner, J J.]]
[[Category: Dna-binding]]
[[Category: Fad]]
[[Category: Flavoenzyme]]
[[Category: Flavoprotein]]
[[Category: Multifunctional enzyme]]
[[Category: Nad]]
[[Category: Oxidoreductase]]
[[Category: Proline metabolism]]
[[Category: Proline utilization some]]
[[Category: Puta]]
[[Category: Repressor]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb  4 11:33:47 2009''

Revision as of 12:33, 4 February 2009

File:3e2q.jpg

Template:STRUCTURE 3e2q

Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with trans-4-hydroxy-L-prolineCrystal Structure Reduced PutA86-630 Mutant Y540S Complexed with trans-4-hydroxy-L-proline

Template:ABSTRACT PUBMED 19140736

About this StructureAbout this Structure

3E2Q is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Ostrander EL, Larson JD, Schuermann JP, Tanner JJ. A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate (dagger) (double dagger). Biochemistry. 2009 Feb 10;48(5):951-9. PMID:19140736 doi:10.1021/bi802094k

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