1qfx

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(New page: 200px<br /><applet load="1qfx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfx, resolution 2.4&Aring;" /> '''PH 2.5 ACID PHOSPHATA...)
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[[Image:1qfx.jpg|left|200px]]<br /><applet load="1qfx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qfx.jpg|left|200px]]<br /><applet load="1qfx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qfx, resolution 2.4&Aring;" />
caption="1qfx, resolution 2.4&Aring;" />
'''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER'''<br />
'''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER'''<br />
==Overview==
==Overview==
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The crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC, 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two, dimers form a tetramer in which the active sites are easily accessible to, substrates. The main contacts in the dimer come from the N termini, each, lying on the surface of the neighbouring molecule. The monomer consists of, two domains, with the active site located at their interface. The active, site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate, specificity of the enzyme.
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The crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two dimers form a tetramer in which the active sites are easily accessible to substrates. The main contacts in the dimer come from the N termini, each lying on the surface of the neighbouring molecule. The monomer consists of two domains, with the active site located at their interface. The active site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate specificity of the enzyme.
==About this Structure==
==About this Structure==
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1QFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with NAG, SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFX OCA].
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1QFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFX OCA].
==Reference==
==Reference==
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[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arcy, A.D.]]
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[[Category: Arcy, A D.]]
[[Category: Kostrewa, D.]]
[[Category: Kostrewa, D.]]
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[[Category: Loon, A.P.G.M.Van.]]
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[[Category: Loon, A P.G M.Van.]]
[[Category: Wyss, M.]]
[[Category: Wyss, M.]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: phosphomonoesterase]]
[[Category: phosphomonoesterase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:39:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:06 2008''

Revision as of 12:39, 21 February 2008


1qfx, resolution 2.4Å

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PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

Overview

The crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two dimers form a tetramer in which the active sites are easily accessible to substrates. The main contacts in the dimer come from the N termini, each lying on the surface of the neighbouring molecule. The monomer consists of two domains, with the active site located at their interface. The active site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate specificity of the enzyme.

About this Structure

1QFX is a Single protein structure of sequence from Aspergillus niger with , and as ligands. Active as 3-phytase, with EC number 3.1.3.8 Full crystallographic information is available from OCA.

Reference

Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution., Kostrewa D, Wyss M, D'Arcy A, van Loon AP, J Mol Biol. 1999 May 21;288(5):965-74. PMID:10329192

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