1F5S: Phosphoserine Phosphatase
Background
Phosphoserine phosphatase (PSP) is an enzyme which produces L-serine, and is then converted to D-serine. D-serine is a co-agonist of the N-methyl-D-aspartate subtype of glutamate receptors, a major neurotransmitter receptor family in mammalian nervous systems. PSP from M. jannaschii shares significant sequence homology with human PSP. PSPs are members of the haloacid dehalogenase (HAD)-like hydrolase family, and all members share three conserved sequence motifs. PSP utilizes a common mechanism that involves Mg(2+)-dependent phosphorylation and autodephosphorylation at an aspartyl side chain in the active site.
M. jannaschii is a thermophilic (48-94 C), strict anaerobic Archaebacterium which lives at pressures of over 200 atmospheres. It is an autotroph which gets its energy from hydrogen and carbon dioxide producing methane and it is capable of nitrogen fixation. Morphologically it is characterized by having two bundles of flagella at the same cellular pole.
More PDB information on 1F5S can be found here