1qhf: Difference between revisions

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New page: left|200px<br /><applet load="1qhf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qhf, resolution 1.7Å" /> '''YEAST PHOSPHOGLYCERAT...
 
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[[Image:1qhf.jpg|left|200px]]<br /><applet load="1qhf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1qhf.jpg|left|200px]]<br /><applet load="1qhf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1qhf, resolution 1.7&Aring;" />
caption="1qhf, resolution 1.7&Aring;" />
'''YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A'''<br />
'''YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A'''<br />


==Overview==
==Overview==
The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate, mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7, A resolution in complex with the sugar substrate. The difference map, indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic, residue, histidine 8.
The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.


==About this Structure==
==About this Structure==
1QHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 and 3PG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QHF OCA].  
1QHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=3PG:'>3PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHF OCA].  


==Reference==
==Reference==
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[[Category: Crowhurst, G.]]
[[Category: Crowhurst, G.]]
[[Category: Littlechild, J.]]
[[Category: Littlechild, J.]]
[[Category: Watson, H.C.]]
[[Category: Watson, H C.]]
[[Category: 3PG]]
[[Category: 3PG]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: transferase (phosphoryl)]]
[[Category: transferase (phosphoryl)]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:40 2008''

Revision as of 12:39, 21 February 2008

File:1qhf.jpg


1qhf, resolution 1.7Å

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YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A

Overview

The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.

About this Structure

1QHF is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 and 3PG as ligands. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 Full crystallographic information is available from OCA.

Reference

Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A., Crowhurst GS, Dalby AR, Isupov MN, Campbell JW, Littlechild JA, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1822-6. PMID:10531478

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