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3m5c
From Proteopedia
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| - | + | [[Image:3m5c.png|left|200px]] | |
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===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302E mutant complexed with PALAO=== | ===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302E mutant complexed with PALAO=== | ||
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| + | The line below this paragraph, {{ABSTRACT_PUBMED_20695527}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 20695527 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_20695527}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3m5c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5C OCA]. | |
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:20695527</ref><references group="xtra"/> | ||
[[Category: N-acetylornithine carbamoyltransferase]] | [[Category: N-acetylornithine carbamoyltransferase]] | ||
[[Category: Xanthomonas campestris pv. campestris]] | [[Category: Xanthomonas campestris pv. campestris]] | ||
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[[Category: Tuchman, M.]] | [[Category: Tuchman, M.]] | ||
[[Category: Yu, X.]] | [[Category: Yu, X.]] | ||
| - | [[Category: Transcarbamylase]] | ||
| - | [[Category: Transferase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:38:10 2010'' | ||
Revision as of 05:25, 12 January 2011
Crystal structure of N-acetyl-L-ornithine transcarbamylase K302E mutant complexed with PALAO
Template:ABSTRACT PUBMED 20695527
About this Structure
3m5c is a 1 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA.
Reference
- Li Y, Yu X, Ho J, Fushman D, Allewell NM, Tuchman M, Shi D. Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry. 2010 Aug 17;49(32):6887-95. PMID:20695527 doi:10.1021/bi1007386
