1qfx | pdb_00001qfx

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

spinqualitylabelsall models 1qfx, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qfx is a 2 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, GOL, NAG, SO4, MAN Activity: 3-phytase, with EC number 3.1.3.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PHYB_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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acid phosphatase

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