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8XAL

Cryo-EM structure of SARS-CoV-2 S-BQ.1 in complex with ACE2

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019064biological_processfusion of virus membrane with host plasma membrane
A0039654biological_processfusion of virus membrane with host endosome membrane
A0046813biological_processreceptor-mediated virion attachment to host cell
A0055036cellular_componentvirion membrane
A0075509biological_processendocytosis involved in viral entry into host cell
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019064biological_processfusion of virus membrane with host plasma membrane
B0039654biological_processfusion of virus membrane with host endosome membrane
B0046813biological_processreceptor-mediated virion attachment to host cell
B0055036cellular_componentvirion membrane
B0075509biological_processendocytosis involved in viral entry into host cell
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
I0006091biological_processgeneration of precursor metabolites and energy
I0006508biological_processproteolysis
I0008218biological_processbioluminescence
I0008237molecular_functionmetallopeptidase activity
I0008241molecular_functionpeptidyl-dipeptidase activity
I0016020cellular_componentmembrane
J0006091biological_processgeneration of precursor metabolites and energy
J0006508biological_processproteolysis
J0008218biological_processbioluminescence
J0008237molecular_functionmetallopeptidase activity
J0008241molecular_functionpeptidyl-dipeptidase activity
J0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ITHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
IGLU375
JGLU375
CGLN685

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
IHIS505
JHIS505
CASP815

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
IARG169
ITRP477
ILYS481
JARG169
JTRP477
JLYS481
CASN17
CASP1158
CASN1173

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
IARG273
BPRO1074
CTRP61
CVAL122
CVAL717
CLEU801
CPRO1074
IHIS345
ITYR515
JARG273
JHIS345
JTYR515
BVAL122
BVAL717
BLEU801

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
IHIS374
IHIS378
IGLU402
JHIS374
JHIS378
JGLU402
CPHE74
CGLU149
CASP1194

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
IASN53
BCYS331
BALA343
BPRO616
BCYS657
BPHE1098
CTYR165
CASP282
CCYS331
CALA343
CPRO616
IASN322
CCYS657
CPHE1098
JASN53
JASN322
APRO616
ACYS657
APHE1098
BTYR165
BASP282

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
IASN90
JASN90
BGLN234
BILE709
CGLN234
CILE709

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
IASN103
IASN432
JASN103
JASN432

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
IASN546
JASN546
CPRO325

site_idSWS_FT_FI10
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
AVAL603
BVAL603
CVAL603

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
AHIS676
ASER678
BHIS676
BSER678
CHIS676
CSER678

site_idSWS_FT_FI12
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
AASP1134
BASP1134
CASP1134

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PDB entries from 2025-06-18

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