Ribonucleoside-diphosphate reductase holoenzyme that provides the precursors necessary for viral DNA synthesis (By similarity). Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). Prevents host necroptosis by targeting host RIPK1 and RIPK3, thereby hampering the formation of necroptotic RIPK1-RIPK3 complexes (PubMed:25674983, PubMed:30050136). Forms hetero-amyloid structures with host proteins RIPK3 or ZBP1 which may prevent RIPK3- and ZBP1-mediated necroptosis (PubMed:33348174). In addition, inhibits extrinsic apoptosis by targeting host CASP8 (PubMed:25674983). [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate Genetic information processing; DNA replication. Heterotetramer composed of a homodimer of the large subunit (R1) and a homodimer of the small subunit (R2) (By similarity). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n (By similarity). Self-assembles (via RIP homotypic interaction motif/RHIM) into homomeric fibrillar amyloid structures (PubMed:33348174). Interacts (via RHIM) with human RIPK1 (via RHIM) (PubMed:25674983). Interacts (via RHIM) with human RIPK3 (via RHIM); the interaction leads to heteromeric amyloid assemblies (PubMed:25316792, PubMed:25674983, PubMed:33348174). Interacts (via RHIM) with human ZBP1 (via RHIM); the interaction leads to heteromeric amyloid assemblies (PubMed:33348174). Interacts (via C-terminus) with host CASP8 (PubMed:25674983). The RIP homotypic interaction motif/RHIM drives self-assembly into homomeric amyloid structures and mediates interaction with the RHIM motif of host proteins RIPK3 and ZBP1 to form heteromeric amyloid structures. Belongs to the ribonucleoside diphosphate reductase large chain family.