2P4D

Structure-assisted discovery of Variola major H1 phosphatase inhibitors

Summary for 2P4D

Entry DOI	10.2210/pdb2p4d/pdb
Descriptor	Dual specificity protein phosphatase (2 entities in total)
Functional Keywords	dual specificity phosphatase, enzyme, small pox, drug design, hydrolase
Biological source	Variola virus
Cellular location	Virion : P33064
Total number of polymer chains	1
Total formula weight	20235.17
Authors	Phan, J.,Tropea, J.E.,Waugh, D.S. (deposition date: 2007-03-12, release date: 2007-05-29, Last modification date: 2024-11-13)
Primary citation	Phan, J.,Tropea, J.E.,Waugh, D.S. Structure-assisted discovery of variola major H1 phosphatase inhibitors Acta Crystallogr.,Sect.D, D63:698-704, 2007 Cited by PubMed Abstract: Variola major virus, the causative agent of smallpox, encodes the dual-specificity H1 phosphatase. Because this enzyme is essential for the production of mature virus particles, it is an attractive molecular target for the development of therapeutic countermeasures for this potential agent of bioterrorism. As a first step in this direction, the crystal structure of H1 phosphatase has been determined at a resolution of 1.8 A. In silico screening methods have led to the identification of several small molecules that inhibit Variola H1 phosphatase with IC(50) values in the low micromolar range. These molecules provide novel leads for future drug development. PubMed: 17505108 DOI: 10.1107/S0907444907014904 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation