2we5: Difference between revisions

Revision as of 10:01, 7 April 2010

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:2we5.png

Template:STRUCTURE 2we5

CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADPCARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP

Template:ABSTRACT PUBMED 10211841

About this StructureAbout this Structure

2WE5 is a 3 chains structure with sequences from Enterococcus faecalis. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}^{[xtra 2]}

↑ Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V. Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine. Protein Sci. 1999 Apr;8(4):934-40. PMID:10211841
↑ Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:10860751 doi:http://dx.doi.org/10.1006/jmbi.2000.3779

Page seeded by OCA on Wed Apr 7 10:01:26 2010

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

OCA

[1] Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V. Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine. Protein Sci. 1999 Apr;8(4):934-40. PMID:10211841

[2] Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:10860751 doi:http://dx.doi.org/10.1006/jmbi.2000.3779

[xtra 1]

[xtra 2]

@@ Line 1: / Line 1: @@
 {{Seed}}
-[[Image:2we5.jpg|left|200px]]
+[[Image:2we5.png|left|200px]]
 <!--
@@ Line 14: / Line 14: @@
 <!--
-The line below this paragraph, {{ABSTRACT_PUBMED_20188742}}, adds the Publication Abstract to the page
+The line below this paragraph, {{ABSTRACT_PUBMED_10211841}}, adds the Publication Abstract to the page
-(as it appears on PubMed at http://www.pubmed.gov), where 20188742 is the PubMed ID number.
+(as it appears on PubMed at http://www.pubmed.gov), where 10211841 is the PubMed ID number.
 -->
-{{ABSTRACT_PUBMED_20188742}}
+{{ABSTRACT_PUBMED_10211841}}
 ==About this Structure==
@@ Line 23: / Line 23: @@
 ==Reference==
-<ref group="xtra">PMID:20188742</ref><ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
+<ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
 [[Category: Carbamate kinase]]
 [[Category: Enterococcus faecalis]]
@@ Line 37: / Line 37: @@
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 17 09:24:36 2010''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  7 10:01:26 2010''