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7XO4

SARS-CoV-2 Omicron BA.1 Variant Spike Trimer with two mouse ACE2 Bound

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
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008241molecular_functionpeptidyl-dipeptidase activity
D0016020cellular_componentmembrane
E0006508biological_processproteolysis
E0008237molecular_functionmetallopeptidase activity
E0008241molecular_functionpeptidyl-dipeptidase activity
E0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
DTHR371-GLN380

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ATSTdyNsRLWAWEG
ChainResidueDetails
DALA153-GLY167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1444
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
DGLN18-THR740
EGLN18-THR740
CSER685

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354
ChainResidueDetails
DILE741-ILE761
EILE741-ILE761
CARG815

site_idSWS_FT_FI3
Number of Residues86
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
DVAL762-PHE805
EVAL762-PHE805
AASN1173
BASN17
BASN1158
BASN1173
CASN17
CASN1158
CASN1173

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
DGLU375
BASN1074
CASN61
CTHR124
CASN717
CASN801
CASN1074
EGLU375
AASN717
AASN801
AASN1074
BASN61
BTHR124
BASN717
BASN801

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
DHIS505
EHIS505
AASN1194
BTHR76
BGLU154
BASN1194
CTHR76
CGLU154
CASN1194

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
DARG169
EGLU402
ETRP477
ELYS481
BASN657
BASN1098
CTYR170
CASN282
CASN331
CASN343
CASN616
DHIS374
CASN657
CASN1098
DHIS378
DGLU402
DTRP477
DLYS481
EARG169
EHIS374
EHIS378

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1
ChainResidueDetails
DARG273
DHIS345
DTYR515
EARG273
EHIS345
ETYR515

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9BYF1
ChainResidueDetails
DTYR781
ETYR781
CTHR323

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9BYF1
ChainResidueDetails
DSER783
ESER783
CSER325

site_idSWS_FT_FI10
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
DASN53
EASN690
DASN536
DASN546
DASN660
DASN690
EASN53
EASN536
EASN546
EASN660

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q9BYF1
ChainResidueDetails
DLYS788
ATHR678
ELYS788
BTHR678
CTHR676
CTHR678

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
AASN1134
BASN1134
CASN1134

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PDB entries from 2024-07-24

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