3gmz
From Proteopedia
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===Crystal of human arginase in complex with L-ornithine. Resolution 1.43 A.=== | ===Crystal of human arginase in complex with L-ornithine. Resolution 1.43 A.=== | ||
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| + | The line below this paragraph, {{ABSTRACT_PUBMED_21728378}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 21728378 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_21728378}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3gmz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GMZ OCA]. | |
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:021728378</ref><references group="xtra"/> | ||
[[Category: Arginase]] | [[Category: Arginase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Costanzo, L Di.]] | [[Category: Costanzo, L Di.]] | ||
[[Category: Arginine metabolism]] | [[Category: Arginine metabolism]] | ||
| - | [[Category: | + | [[Category: Hydrolase-hydrolase inhibitor complex]] |
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Ornithine binding]] | [[Category: Ornithine binding]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
| - | [[Category: Polymorphism]] | ||
[[Category: Urea cycle]] | [[Category: Urea cycle]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 27 19:59:52 2010'' | ||
Revision as of 06:46, 20 July 2011
Crystal of human arginase in complex with L-ornithine. Resolution 1.43 A.
Template:ABSTRACT PUBMED 21728378
About this Structure
3gmz is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Ilies M, Di Costanzo L, Dowling DP, Thorn KJ, Christianson DW. Binding of alpha,alpha-Disubstituted Amino Acids to Arginase Suggests New Avenues for Inhibitor Design. J Med Chem. 2011 Jul 18. PMID:21728378 doi:10.1021/jm200443b
