1qhf

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(New page: 200px<br /><applet load="1qhf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qhf, resolution 1.7&Aring;" /> '''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"
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[[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==
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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.
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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==
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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].
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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.]]
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[[Category: Watson, H.C.]]
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[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:41:50 2007''
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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


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 and 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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