1qfx
From Proteopedia
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | 3-phytase, with EC number 3.1.3.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:36:54 2008
Categories: 3-phytase | Aspergillus niger | Single protein | Arcy, A D. | Kostrewa, D. | Loon, A P.G M.Van. | Wyss, M. | GOL | NAG | SO4 | Phosphomonoesterase
