Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins. Homomultimer. Makes the hexons and eleven out of twelve pentons. Interacts with triplex proteins 1/TRX1 and 2/TRX2; adjacent capsomers are linked together in groups of three by triplexes, heterotrimeric complexes composed of one molecule of TRX1 and two molecules of TRX2. Interacts with scaffold protein; this interaction allows efficient MCP transport to the host nucleus. Interacts with capsid vertex component 2/CVC2. Interacts with the small capsomere-interacting protein/SCP. Belongs to the herpesviridae major capsid protein family.