EC Number   |
|---|
  4.2.1.168 | H188N mutant with bound GDP-perosamine, to 1.7 A resolution. The sugar analog is trapped in the active site as an external aldimine. The active site is positioned between the two subunits of the dimer. The diphosphoryl groups of the ligand are anchored to the protein via Arg219 and Arg331, the hydroxyl groups of the hexose only lie within hydrogen bonding distance to ordered water molecules. The hexose moiety of the ligand adopts a boat rather than the typically observed chair conformation |
| 4.2.1.168 | mutant H188K in the presence of alpha-ketoglutarate and pyridoxal 5'-phosphate, to 1.9 A resolution. The observed electron density is consistent with the formation of a geminal diamine intermediate formed by the reaction of an internal aldimine with glutamate |
| 4.2.1.168 | the two subunits of the protein form a tight dimer. The PLP-binding pocket is formed primarily by one subunit, with a loop from Phe 240 to Glu 253 in the second subunit, that completes the active site architecture. The hydrated form of PLP is observed. Amino acid residues involved in anchoring the cofactor to the protein include Gly56, Ser57, Asp159, Glu162, and Ser183 from one subunit and Asn248 from the second monomer. His188 is the active site base required for catalysis |
