1nc1: Difference between revisions

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[[Image:1nc1.jpg|left|200px]]<br /><applet load="1nc1" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nc1.jpg|left|200px]]
caption="1nc1, resolution 2.00&Aring;" />
 
'''Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)'''<br />
{{Structure
|PDB= 1nc1 |SIZE=350|CAPTION= <scene name='initialview01'>1nc1</scene>, resolution 2.00&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MTH:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-METHYLSULFANYLMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>MTH</scene>
|ACTIVITY=
|GENE= MTN OR PFS OR B0159 OR Z0170 OR ECS0163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1NC1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MTH:'>MTH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NC1 OCA].  
1NC1 is a [[Single protein]] 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=1NC1 OCA].  


==Reference==
==Reference==
Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis., Lee JE, Cornell KA, Riscoe MK, Howell PL, J Biol Chem. 2003 Mar 7;278(10):8761-70. Epub 2002 Dec 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12496243 12496243]
Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis., Lee JE, Cornell KA, Riscoe MK, Howell PL, J Biol Chem. 2003 Mar 7;278(10):8761-70. Epub 2002 Dec 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12496243 12496243]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: mixed alpha/beta dimer]]
[[Category: mixed alpha/beta dimer]]


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