1t5h

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[[Image:1t5h.png|left|200px]]
[[Image:1t5h.png|left|200px]]
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{{STRUCTURE_1t5h| PDB=1t5h | SCENE= }}
{{STRUCTURE_1t5h| PDB=1t5h | SCENE= }}
===4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine===
===4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine===
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{{ABSTRACT_PUBMED_15236575}}
{{ABSTRACT_PUBMED_15236575}}
==About this Structure==
==About this Structure==
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1T5H is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_sp._al3007 Alcaligenes sp. al3007]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5H OCA].
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[[1t5h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_sp._al3007 Alcaligenes sp. al3007]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5H OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:15236575</ref><references group="xtra"/>
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<ref group="xtra">PMID:015236575</ref><references group="xtra"/>
[[Category: 4-chlorobenzoate--CoA ligase]]
[[Category: 4-chlorobenzoate--CoA ligase]]
[[Category: Alcaligenes sp. al3007]]
[[Category: Alcaligenes sp. al3007]]
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[[Category: Lu, X.]]
[[Category: Lu, X.]]
[[Category: Adenylate-forming coenzyme a ligase domain alternation conformational change]]
[[Category: Adenylate-forming coenzyme a ligase domain alternation conformational change]]
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[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:43:10 2009''
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Revision as of 12:57, 5 January 2013

Template:STRUCTURE 1t5h

4-Chlorobenzoyl-CoA Ligase/Synthetase unliganded, selenomethionine

Template:ABSTRACT PUBMED 15236575

About this Structure

1t5h is a 1 chain structure with sequence from Alcaligenes sp. al3007. Full crystallographic information is available from OCA.

Reference

  • Gulick AM, Lu X, Dunaway-Mariano D. Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states. Biochemistry. 2004 Jul 13;43(27):8670-9. PMID:15236575 doi:10.1021/bi049384m

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