1qfx | pdb_00001qfx

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Revision as of 22:32, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1qfx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfx, resolution 2.4Å" /> '''PH 2.5 ACID PHOSPHATA...)
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File:1qfx.jpg


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 NAG, SO4 and GOL 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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