1qfx
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PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER
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Structural highlights
FunctionPHYB_ASPAW Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 23:47, 27 December 2023.