1ps1 is a 2 chain structure with sequence from Streptomyces sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.
Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.,Lesburg CA, Zhai G, Cane DE, Christianson DW Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Lesburg CA, Zhai G, Cane DE, Christianson DW. Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology. Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272
