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7YR2

SARS-CoV-2 BA.2.75 S Trimer in complex with ACE2(state1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019064biological_processfusion of virus membrane with host plasma membrane
C0039654biological_processfusion of virus membrane with host endosome membrane
C0046813biological_processreceptor-mediated virion attachment to host cell
C0055036cellular_componentvirion membrane
C0075509biological_processendocytosis involved in viral entry into host cell
D0016020cellular_componentmembrane
D0019031cellular_componentviral envelope
D0019064biological_processfusion of virus membrane with host plasma membrane
D0039654biological_processfusion of virus membrane with host endosome membrane
D0046813biological_processreceptor-mediated virion attachment to host cell
D0055036cellular_componentvirion membrane
D0075509biological_processendocytosis involved in viral entry into host cell
E0016020cellular_componentmembrane
E0019031cellular_componentviral envelope
E0019064biological_processfusion of virus membrane with host plasma membrane
E0039654biological_processfusion of virus membrane with host endosome membrane
E0046813biological_processreceptor-mediated virion attachment to host cell
E0055036cellular_componentvirion membrane
E0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ATHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3597
DetailsTOPO_DOM: Extracellular => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
DGLN17-ILE1216
EGLN17-ILE1216
CGLN17-ILE1216

site_idSWS_FT_FI2
Number of Residues60
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
DTRP1217-MET1237
ETRP1217-MET1237
CTRP1217-MET1237

site_idSWS_FT_FI3
Number of Residues114
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
AARG169
ATRP477
ALYS481

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Cleavage; by host furin => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
DALA688
EALA688
CALA688

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
DILE818
EILE818
CILE818

site_idSWS_FT_FI6
Number of Residues15
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20 => ECO:0000269|PubMed:34599882
ChainResidueDetails
DTHR1238
EGLY1246
CTHR1238
CSER1239
CCYS1243
CLEU1244
CGLY1246
DSER1239
DCYS1243
DLEU1244
DGLY1246
ETHR1238
ESER1239
ECYS1243
ELEU1244

site_idSWS_FT_FI7
Number of Residues15
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20; partial => ECO:0000269|PubMed:34599882
ChainResidueDetails
DCYS1250
EASP1257
CCYS1250
CGLY1251
CCYS1253
CPHE1256
CASP1257
DGLY1251
DCYS1253
DPHE1256
DASP1257
ECYS1250
EGLY1251
ECYS1253
EPHE1256

site_idSWS_FT_FI8
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DASN20
DSER1161
DVAL1176
EASN20
ESER1161
EVAL1176
CASN20
CSER1161
CVAL1176

site_idSWS_FT_FI9
Number of Residues15
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DTRP64
ETHR1077
CTRP64
CASN125
CILE720
CGLN804
CTHR1077
DASN125
DILE720
DGLN804
DTHR1077
ETRP64
EASN125
EILE720
EGLN804

site_idSWS_FT_FI10
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DLYS77
DARG152
DLEU1197
ELYS77
EARG152
ELEU1197
CLYS77
CARG152
CLEU1197

site_idSWS_FT_FI11
Number of Residues21
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DPHE168
EASN334
EARG346
EGLU619
ETYR660
EHIS1101
CPHE168
CILE285
CASN334
CARG346
CGLU619
DILE285
CTYR660
CHIS1101
DASN334
DARG346
DGLU619
DTYR660
DHIS1101
EPHE168
EILE285

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DARG237
DILE712
EARG237
EILE712
CARG237
CILE712

site_idSWS_FT_FI13
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
DILE326
EILE326
CILE326

site_idSWS_FT_FI14
Number of Residues3
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
DARG328
EARG328
CARG328

site_idSWS_FT_FI15
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DASN606
EASN606
CASN606

site_idSWS_FT_FI16
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
DLYS679
DHIS681
ELYS679
EHIS681
CLYS679
CHIS681

site_idSWS_FT_FI17
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
DVAL1137
EVAL1137
CVAL1137

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PDB entries from 2025-06-11

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