1IDP

Crystal structure of scytalone dehydratase F162A mutant in the unligated state

Summary for 1IDP

Entry DOI	10.2210/pdb1idp/pdb
Related	3std 4std 5std 6std 7std
Descriptor	SCYTALONE DEHYDRATASE (1 entity in total)
Functional Keywords	lyase, melanine biosynthesis
Biological source	Magnaporthe grisea
Total number of polymer chains	3
Total formula weight	60614.42
Authors	Nakasako, M.,Motoyama, T.,Yamaguchi, I. (deposition date: 2001-04-04, release date: 2003-04-08, Last modification date: 2023-10-25)
Primary citation	Motoyama, T.,Nakasako, M.,Yamaguchi, I. Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K Acta Crystallogr.,Sect.D, 58:148-150, 2002 Cited by PubMed Abstract: Scytalone dehydratase variant F162A, in which Phe162 in the C-terminal region was replaced with alanine, was crystallized with polyethylene glycol 4000. Because the crystal was radiation-sensitive, the diffraction data were collected at cryogenic temperatures. The crystal belonged to monoclinic space group P2(1), with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 A, beta = 120.02 degrees at 37 K. The calculated V(M) value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 A at BL41XU of SPring-8 at 37 K. PubMed: 11752795 DOI: 10.1107/S0907444901017371 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.45 Å)

Structure validation