Table 1. Available Structures (X-ray, NMR, or EM) are from 17 Proteins Encoded in the SARS-CoV-2 Genome and Three Proteins Encoded in the SARS-CoV Genome^a.

protein	description	experimental structures at PDB
NSP1	inhibits host translation by interacting with the 40S ribosomal subunit42	SARS-CoV-2; 7JQB (cryoEM), 7K7P and 7K3N
NSP2	involved in the disruption of intracellular host signaling during SARS-CoV infections43
NSP3	multidomain protein including the papain-like protease domain; involved in cutting the N-terminal part of PP1a and PP1ab to mature NSP1, NSP2, and NSP3 itself and altering many of the infected host proteins; interacts with NSP429	SARS-CoV-2; PLpro domain (6WUU, 6WX4, 6W9C, 6WZU, 6YVA, 6WRH, 7KRX, 7KOK, and 7D6H), ARH domain (6WOJ, 6WEY, 6YWK, 6YWL, 6YWM, 6WEN, 6VXS, 6W02, 6WCF, 6W6Y, 7KXB, 7LG7, 6Z5T, 7BF5, 7C33, 7CZ4, and 7KG3)
NSP4	forms virally induced cytoplasmic double-membrane vesicles necessary for viral replication44
NSP5	3C-like protease maturing most of the NSPs (NSP4–NSP16) from PP1ab33,34,45−48	SARS-CoV-2; 137 structures (6LU7, 6M2Q, and 135 more)
NSP6	forms virally induced cytoplasmic double-membrane vesicles necessary for viral replication44
NSP7	cofactor of RNA-dependent RNA polymerase (NSP12)35,49,50	SARS-CoV-2; 7BV1, 7BW4, 7BV2, 6WTC, 6WIQ, 6WQD, 6M71, 7BTF, 6YYT, 6YHU, and 7DCD
NSP8	cofactor of RNA-dependent RNA polymerase (NSP12)35,49,50	SARS-CoV-2; 7BV1, 7BW4, 7BV2, 6WTC, 6WIQ, 6WQD, 6M71, 7BTF, 6YYT, 6YHU, and 7DCD
NSP9	single-stranded RNA-binding protein; interacts with NSP836	SARS-CoV-2; 6W4B, 6WXD, and 6W9Q
NSP10	critical co-factor for the activity of 3′ → 5′ exonuclease (NSP14) and 2′-O-ribose methyltransferase (NSP16)51	SARS-CoV-2; 6WKQ, 7C2J, 7C2I, 6WKS, 6W61, 6WVN, 6WQ3, 6WJT, 6WRZ, 6W4H, 6W75, 6YZ1, 7KOA, 7L6T, 6ZPE, and 6ZCT
NSP11	the leftover of PP1a fragmentation52
NSP12	RNA-dependent RNA polymerase, responsible for replication and transcription of the viral RNA genome35,49,50,53	SARS-CoV-2; 7BTF, 7BV1, 7BV2, 6YYT, 7BW4, 7L1F, 7B3B, and 7D4F
NSP13	helicase; interacts with NSP1254	SARS-CoV-2; 7NN0 and 7NIO
NSP14	N-terminal 3′ → 5′ exonuclease domain and C-terminal N7-guanine-methyltransferase domain51	SARS-CoV; 5C8U, 5C8S, 5C8T, and 5NFY
NSP15	uridylate-specific endoribonuclease55,56	SARS-CoV-2; 6W01, 6WXC, 6WLC, 6X1B, 6VWW, 7K0R, 7KEG, 5S71, 7K1O, and 7K9P
NSP16	2′-O-ribose methyltransferase mediating the 5′-cap structure of viral mRNAs39,51	SARS-CoV-2; 6WKQ, 7C2J, 7C2I, 6WKS, 6W61, 6WVN, 6WQ3, 6WJT, 6WRZ, 6W4H, 6W75, 6YZ1, 7KOA, and 7L6T
S	spike glycoprotein interacting with the host receptor protein ACE212,13,40,57−61	SARS-CoV-2; receptor-binding domain (6VSB, 7BZ5, 6M0J, 6M17, 6W41, 7C01, 6LZG, 6YM0, 6YLA, 6YOR, and 6VW1), S2 domain (6LXT and 6LVN), cryoEM of the full-length (6VXX, 6WPT, 6WPS, 6VYB, 6X29, 6X2C, 6X2A, and 6X2B)
ORF3a	accessory protein; activates the NLRP3 inflammasome62	SARS-CoV-2; 7KJR (cryoEM)
ORF3b	accessory protein; IFN antagonist6
E	envelope protein; mediates virus morphogenesis and assembly63,64	SARS-CoV; 5X29 and 2MM4
M	membrane glycoprotein; involved in virus morphogenesis and assembly44,63
ORF6	accessory protein; antagonizes type I interferon65
ORF7a	accessory protein; inhibits the antiviral function of bone marrow stromal antigen 2 (BST-2)66	SARS-CoV-2; 6W37 and 7CI3
ORF7b	accessory protein and a structural component of the SARS-CoV virion67	SARS-CoV; 6W37
ORF8	accessory protein; important for interspecies transmission of the virus; activates the NLRP3 inflammasome68,69	SARS-CoV-2; 7JX6
ORF9b	accessory protein; suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome70	SARS-CoV-2; 7KDT (cryoEM)
ORF9c	unknown52
N	nucleocapsid phosphoprotein; packages the viral RNA genome41,71	SARS-CoV-2; N-terminal RNA-binding domain (6YI3, 6M3M, 6WKP, 6VYO, and 7CR5), C-terminal dimerization domain (6WZQ, 6WZO, 6WJI, 6YUN, and 7C22)
ORF10	unknown; may not be produced7

^aPDB code(s) of the structures are listed for each protein, when available, together with the attributed functions for the viral proteins.