1qfx
From Proteopedia
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'''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER''' | '''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER''' | ||
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[[Category: Loon, A P.G M.Van.]] | [[Category: Loon, A P.G M.Van.]] | ||
[[Category: Wyss, M.]] | [[Category: Wyss, M.]] | ||
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Revision as of 03:13, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 06:13:16 2008