| Primary Identifier | IPR029066 | Type | Homologous_superfamily |
| Short Name | PLP-binding_barrel |
| description | This entry represents the PLP (pyridoxal 5'-phosphate)-binding barrel that can be found at the N terminus of alanine racemase-like proteins and members of the Orn/Lys/Arg decarboxylase class-II family of proteins.The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A []. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N terminus, and a C-terminal domain essentially composed of β-strands. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the α/β barrel and is covalently linked via an aldimine linkage to a lysine residue, which is at the C terminus of the first β-strand of the α/β barrel. |
