2ggk: Difference between revisions

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[[Image:2ggk.gif|left|200px]]<br /><applet load="2ggk" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2ggk.gif|left|200px]]
caption="2ggk, resolution 2.30&Aring;" />
 
'''The mutant A302C of Agrobacterium radiobacter N-carbamoyl-D-amino-acid amidohydrolase'''<br />
{{Structure
|PDB= 2ggk |SIZE=350|CAPTION= <scene name='initialview01'>2ggk</scene>, resolution 2.30&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/N-carbamoyl-D-amino_acid_hydrolase N-carbamoyl-D-amino acid hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.77 3.5.1.77]
|GENE=
}}
 
'''The mutant A302C of Agrobacterium radiobacter N-carbamoyl-D-amino-acid amidohydrolase'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2GGK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. This structure supersedes the now removed PDB entries 2FKV and 2BA5. Active as [http://en.wikipedia.org/wiki/N-carbamoyl-D-amino_acid_hydrolase N-carbamoyl-D-amino acid hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.77 3.5.1.77] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGK OCA].  
2GGK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. This structure supersedes the now removed PDB entries 2FKV and 2BA5. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGK OCA].  


==Reference==
==Reference==
Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase., Chiu WC, You JY, Liu JS, Hsu SK, Hsu WH, Shih CH, Hwang JK, Wang WC, J Mol Biol. 2006 Jun 9;359(3):741-53. Epub 2006 Apr 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16650857 16650857]
Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase., Chiu WC, You JY, Liu JS, Hsu SK, Hsu WH, Shih CH, Hwang JK, Wang WC, J Mol Biol. 2006 Jun 9;359(3):741-53. Epub 2006 Apr 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16650857 16650857]
[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
[[Category: N-carbamoyl-D-amino acid hydrolase]]
[[Category: N-carbamoyl-D-amino acid hydrolase]]
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[[Category: n-carbamoyl-d-amino-acid amidohydrolase]]
[[Category: n-carbamoyl-d-amino-acid amidohydrolase]]


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