1pkm

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(New page: 200px<br /><applet load="1pkm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pkm, resolution 2.6&Aring;" /> '''THE REFINED THREE-DIM...)
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[[Image:1pkm.jpg|left|200px]]<br /><applet load="1pkm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pkm, resolution 2.6&Aring;" />
caption="1pkm, resolution 2.6&Aring;" />
'''THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS'''<br />
'''THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS'''<br />
==Overview==
==Overview==
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The three-dimensional structure of cat-muscle pyoruvate kinase has been, refined at a resolution of 2.6 A. The details of the structure permit, interpretation of the original heavy-atom studies and give insight into, the importance of conserved residues in pyruvate kinases and the, allosteric behaviour of the enzyme. There are a small number of essential, residues which determine the relative orientations of domains and the, precise nature of intersubunit contacts. Arginine residues are, particularly important.
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The three-dimensional structure of cat-muscle pyoruvate kinase has been refined at a resolution of 2.6 A. The details of the structure permit interpretation of the original heavy-atom studies and give insight into the importance of conserved residues in pyruvate kinases and the allosteric behaviour of the enzyme. There are a small number of essential residues which determine the relative orientations of domains and the precise nature of intersubunit contacts. Arginine residues are particularly important.
==About this Structure==
==About this Structure==
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1PKM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Felis_catus Felis catus]. Active as [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PKM OCA].
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1PKM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Felis_catus Felis catus]. Active as [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKM OCA].
==Reference==
==Reference==
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[[Category: Pyruvate kinase]]
[[Category: Pyruvate kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Allen, S.C.]]
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[[Category: Allen, S C.]]
[[Category: Muirhead, H.]]
[[Category: Muirhead, H.]]
[[Category: pyruvate kinase]]
[[Category: pyruvate kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:53:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:47 2008''

Revision as of 12:29, 21 February 2008


1pkm, resolution 2.6Å

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THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS

Overview

The three-dimensional structure of cat-muscle pyoruvate kinase has been refined at a resolution of 2.6 A. The details of the structure permit interpretation of the original heavy-atom studies and give insight into the importance of conserved residues in pyruvate kinases and the allosteric behaviour of the enzyme. There are a small number of essential residues which determine the relative orientations of domains and the precise nature of intersubunit contacts. Arginine residues are particularly important.

About this Structure

1PKM is a Single protein structure of sequence from Felis catus. Active as Pyruvate kinase, with EC number 2.7.1.40 Full crystallographic information is available from OCA.

Reference

Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A., Allen SC, Muirhead H, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):499-504. PMID:15299671

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