1cm2: Difference between revisions

Revision as of 00:51, 18 February 2009

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1cm2.png

Template:STRUCTURE 1cm2

STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.

Template:ABSTRACT PUBMED 10419492

About this StructureAbout this Structure

1CM2 is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Napper S, Delbaere LT, Waygood EB. The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization. J Biol Chem. 1999 Jul 30;274(31):21776-82. PMID:10419492

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Napper S, Delbaere LT, Waygood EB. The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization. J Biol Chem. 1999 Jul 30;274(31):21776-82. PMID:10419492

[xtra 1]

@@ Line 20: / Line 20: @@
 ==About this Structure==
-CM2 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=1CM2 OCA].
+CM2 is a 1 chain 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=1CM2 OCA].
 ==Reference==
-The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization., Napper S, Delbaere LT, Waygood EB, J Biol Chem. 1999 Jul 30;274(31):21776-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10419492 10419492]
+<ref group="xtra">PMID:10419492</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
 [[Category: Delbaere, L T.J.]]
 [[Category: Napper, S.]]
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 [[Category: Succinimide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:56:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:51:05 2009''