1QFX

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

Summary for 1QFX

• Entry DOI: 10.2210/pdb1qfx/pdb
• Descriptor: PROTEIN (PH 2.5 ACID PHOSPHATASE), alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: phosphomonoesterase, hydrolase
• Biological source: Aspergillus niger
• Total number of polymer chains: 2
• Total formula weight: 106399.79

Authors

Kostrewa, D.,Wyss, M.,D'Arcy, A.,Van Loon, A.P.G.M. (deposition date: 1999-04-15, release date: 2000-04-19, Last modification date: 2023-12-27)

Primary citation

Kostrewa, D.,Wyss, M.,D'Arcy, A.,van Loon, A.P.
Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution.
J.Mol.Biol., 288:965-974, 1999

PubMed Abstract: 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.

PubMed: 10329192
DOI: 10.1006/jmbi.1999.2736

Experimental method

X-RAY DIFFRACTION (2.4 Å)