| Type: | Binding_site | Name: | PPM-type phosphatase, divalent cation binding |
| Description: | Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes andprokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphataseMg(2+)- or Mn(2+)-dependent (PPM) families. The core structure of PPMs is the 300-residue PPM-type phosphatase domain that catalyzes the dephosphorylationof phosphoserine- and phosphothreonine-containing protein. The PPM-type phosphatase domain is found as a module in diverse structural contexts and ismodulated by targeting and regulatory subunits [, , , ].The PP2C-type phosphatase domain consists of 10 segments of beta-strands and 5 segments of alpha-helix and comprises a pair of detached subdomains. The firstis a small beta-sandwich with strand beta1 packed against strands beta2 and beta3; the second is a larger beta-sandwich in which a four-stranded beta-heet packs against a three-stranded beta-sheet with flanking alpha-helices [, ].This entry represents a conserved aspartate residue involved in divalent cation binding []. | Short Name: | PP2C_BS |
