At least 30% of proteins contain a metal ion for catalysis, structure, or regulation. In addition to these roles of metal ions in proteins, numerous proteins make coordination environments either rigid or flexible for controlling transport, storage, sensing, and transfer of metal ions. In many of these metal-protein interactions, the coordination environment is not static but dynamic with mechanisms for dissociation and association to move metal ions on a timescale from seconds to years. The second coordination sphere and the protein matrix, which provides hydrophilic or hydrophobic environments, also influence coordination. Despite the limited number of amino acids that can serve as ligands with oxygen, nitrogen and sulfur donor atoms in their side chains, a great variety of structures is accomplished. Beyond the effect of protein dynamics on metal-protein interactions, numerous biological factors determine structure and function. Since many investigations are performed with isolated metalloproteins, most of the biological factors including interactions with other proteins are often not considered. Therefore, taking three different families of mammalian zinc proteins with zinc-thiolate coordination as an example, this short account discusses how the intracellular or extracellular biological environment adds additional layers of coordination dynamics. Interpretation of structure and function requires a lot of information about the conditions and spatiotemporal changes under which metalloproteins work. This information is not always available when investigations of a novel metalloprotein are begun. Addressing the biological context should be a goal in biological inorganic chemistry and considered in the methodology employed for investigations.