Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTrypsin-like serine proteases 8076481 3000114 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APeptidase_C30_Ne2bx4A1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrelF: Peptidase_C30_NECOD (1.6)
APeptidase_C30_Ce2bx4A2 A: alpha arraysX: Coronavirus main proteinase (3Cl-pro, putative coronavirus nsp2) C-terminal domain (From Topology)H: Coronavirus main proteinase (3Cl-pro, putative coronavirus nsp2) C-terminal domain (From Topology)T: Coronavirus main proteinase (3Cl-pro, putative coronavirus nsp2) C-terminal domainF: Peptidase_C30_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.40.10.10 Mainly Beta Beta Barrel Thrombin, subunit H Trypsin-like serine proteasesCATH (4.3.0)
A1.10.1840.10 Mainly Alpha Orthogonal Bundle main proteinase (3clpro) structure, domain 3 main proteinase (3clpro) structure, domain 3CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF05409Coronavirus endopeptidase C30 (Peptidase_C30)Coronavirus endopeptidase C30- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
3C-like proteinase nsp5

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR022733DPUP/SUD, C-terminal, betacoronavirusDomain
IPR042515Non-structural protein NSP15, N-terminal domain superfamily, coronavirusHomologous Superfamily
IPR043174Non-structural protein NSP15, middle domain superfamilyHomologous Superfamily
IPR044315Nonstructural protein 14, betacoronavirusDomain
IPR038123Non-structural protein NSP4, C-terminal superfamily, coronavirusHomologous Superfamily
IPR042570Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirusHomologous Superfamily
IPR043178Papain-like protease, thumb domain superfamily, coronavirusHomologous Superfamily
IPR046441RNA-dependent RNA polymerase, coronavirusDomain
IPR044863Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domainDomain
IPR044343Nonstructural protein 13, 1B domain, coronavirusDomain
IPR038166Polyprotein cleavage domain PL2pro superfamily, betacoronavirusHomologous Superfamily
IPR037227Endoribonuclease EndoU-likeHomologous Superfamily
IPR027352Nonstructural protein 13, zinc-binding domain, coronavirus-likeDomain
IPR009003Peptidase S1, PA clanHomologous Superfamily
IPR013016Peptidase C16, coronavirusDomain
IPR009466Non-structural protein 14, coronavirusDomain
IPR044357NSP3, first ubiquitin-like (Ubl) domain, coronavirusDomain
IPR046436Nidovirus 3'-5' exoribonuclease domainDomain
IPR047570NSP12, interface domain, coronavirusDomain
IPR018995RNA synthesis protein NSP10, coronavirusDomain
IPR043615Nonstructural protein 2, N-terminal domain, coronavirusDomain
IPR050534Coronaviruses polyprotein 1abFamily
IPR043177Papain-like protease, N-terminal domain superfamily, coronavirusHomologous Superfamily
IPR043606Coronavirus replicase NSP15, N-terminal oligomerizationDomain
IPR044330Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirusDomain
IPR041679DNA2/NAM7 helicase-like, C-terminalDomain
IPR024375Non-structural protein NSP3, SUD-M domain, betacoronavirusDomain
IPR014828Non-structural protein NSP7, coronavirusDomain
IPR043503Papain-like viral protease, palm and finger domains, coronavirusHomologous Superfamily
IPR014829Non-structural protein NSP8, coronavirusDomain
IPR036499Non-structural protein NSP9 superfamily, coronavirusHomologous Superfamily
IPR029063S-adenosyl-L-methionine-dependent methyltransferase superfamilyHomologous Superfamily
IPR044389Non-structural protein 2, SARS-CoV-likeDomain
IPR043502DNA/RNA polymerase superfamilyHomologous Superfamily
IPR008740Peptidase C30, coronavirusDomain
IPR036333RNA synthesis protein NSP10 superfamily, coronavirusHomologous Superfamily
IPR047573Non-structural protein 2, middle domain, coronavirusDomain
IPR049894Coronavirus NSP3, 3Ecto domainDomain
IPR043472Macro domain-likeHomologous Superfamily
IPR043609NendoU domain, nidovirusDomain
IPR032592Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirusDomain
IPR043613Non-structural protein 2, C-terminal domain, coronavirusDomain
IPR038083Non-structural protein NSP3A domain-like superfamilyHomologous Superfamily
IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
IPR044351RNA-dependent RNA polymerase, SARS-CoV-likeDomain
IPR024358Non-structural protein NSP3, N-terminal, betacoronavirusDomain
IPR048673Nonstructural protein 13, stalk domain, coronavirusDomain
IPR046435NSP14, guanine-N7-methyltransferase domain, coronavirusDomain
IPR009469RNA-dependent RNA polymerase, N-terminal, coronavirusDomain
IPR043611Coronavirus replicase NSP3, C-terminalDomain
IPR044864Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirusDomain
IPR047566Coronavirus replicase NSP3, Y domainDomain
IPR048672Nonstructural protein 13, zinc-binding domain, coronavirusDomain
IPR043612Non-structural protein NSP4, N-terminal, coronavirusDomain
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
IPR043608Nonstructural protein 15, middle domain, coronavirusDomain
IPR044353NSP3, second ubiquitin-like (Ubl) domain, coronavirusDomain
IPR037204Non-structural protein NSP7 superfamily, coronavirusHomologous Superfamily
IPR044374Non-structural protein 3, SUD-N macrodomain, SARS-CoVDomain
IPR046443NSP1, globular domain, alpha/betacoronavirusDomain
IPR043610Non-structural protein 6, coronavirusDomain
IPR027351(+) RNA virus helicase core domainDomain
IPR044322Nonstructural protein 15, middle domain, alpha/betacoronavirusDomain
IPR009461Non-structural protein NSP16, coronavirus-likeDomain
IPR043477Peptidase C30, domain 3, coronavirusHomologous Superfamily
IPR043478Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirusHomologous Superfamily
IPR038400Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirusHomologous Superfamily
IPR046442NSP1, C-terminal domain, betacoronavirusDomain
IPR001205RNA-directed RNA polymerase, C-terminal domainDomain
IPR044401NSP15, NendoU domain, coronavirusDomain
IPR014822Non-structural protein NSP9, coronavirusDomain
IPR038030NSP1 globular domain superfamily, betacoronavirusHomologous Superfamily
IPR021590NSP1, globular domain, betacoronavirusDomain
IPR044367Non-structural protein 6, betacoronavirusDomain
IPR037230Non-structural protein NSP8 superfamily, coronavirusHomologous Superfamily
IPR046440Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domainDomain
IPR032505Non-structural protein NSP4, C-terminal, coronavirusDomain
IPR046438Nidovirus 2-O-methyltransferaseDomain
IPR002589Macro domainDomain
IPR047567Non-structural protein NSP3, group 2-specific marker domain, betacoronavirusDomain
IPR044371Non-structural protein 3, X-domain-likeDomain
IPR007094RNA-directed RNA polymerase, catalytic domainDomain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
ubiquitinyl hydrolase 1 (peptidase C30 type)  M-CSA #830

The SARS coronavirus main protease dimer (Mpro) is the key enzyme in the processing of the viral polyproteins and thus an attractive target for the discovery of drugs against SARS. The SARS CoV main protease is a cysteine proteinase with a chymostrypsin-like fold. The enzyme cleaves the two overlapping translation products of the SARS coronavirus replicase gene. Hence, inhibition of Mpro leads to prevention of the proteolytic processing of coronavirus replicase polyproteins, stopping the production of of infectious virus particles. The dimer is the enzymatically active species and the conformational state of Mpro is highly pH-sensitive due to the pH-dependence of the protonation state of two histidine residues in the substrate binding site.

Defined by 3 residues: HIS:A-41GLY:A-143CYS:A-145
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Explore in 3DM-CSA Motif Definition