1xbz: Difference between revisions

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[[Image:1xbz.gif|left|200px]]<br /><applet load="1xbz" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1xbz.gif|left|200px]]
caption="1xbz, resolution 1.80&Aring;" />
 
'''Crystal structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/R139V/T169A mutant with bound L-xylulose 5-phosphate'''<br />
{{Structure
|PDB= 1xbz |SIZE=350|CAPTION= <scene name='initialview01'>1xbz</scene>, resolution 1.80&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=LX1:L-XYLULOSE 5-PHOSPHATE'>LX1</scene>
|ACTIVITY=
|GENE= UlaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/R139V/T169A mutant with bound L-xylulose 5-phosphate'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1XBZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=LX1:'>LX1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBZ OCA].  
1XBZ is a [[Protein complex]] structure of sequences 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=1XBZ OCA].  


==Reference==
==Reference==
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase., Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I, Biochemistry. 2005 Feb 15;44(6):1816-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15697207 15697207]
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase., Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I, Biochemistry. 2005 Feb 15;44(6):1816-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697207 15697207]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: tim barrel]]
[[Category: tim barrel]]


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