The distribution and local structural order of hydration water in the proximity of intrinsically disordered proteins/regions are investigated within the frame work of three-dimensional (3D)-reference interaction site model theory. The hydration water distribution around the protein surface is quantified in terms of the 3D distribution function and the water protein radial distribution function (RDF), whereas the local ordering of water molecules around the protein surface is measured in terms of the tetrahedral order parameter. To the best of our knowledge, this is the first theoretical study of the 3D hydration water distribution profiles of disordered proteins. The analysis of the 3D hydration profiles reveals a nonuniform distribution and higher hydration water density around disordered proteins as compared to the globular ones because of their noncompact structures with more solvent-accessible surface area and the abundance of charged residues. This difference is also evident in the residue-specific RDFs of water around different polar and nonpolar atoms of charged and hydrophobic residues of the globular and disordered proteins. The average tetrahedral order parameter evaluated as a function of the water water distance shows that water molecules are more ordered around disordered regions/proteins because of their higher mean net charge facilitating stronger water protein interactions.