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7XO8

SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with three human 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
F0006508biological_processproteolysis
F0008237molecular_functionmetallopeptidase activity
F0008241molecular_functionpeptidyl-dipeptidase activity
F0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
DTHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2166
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
DGLN18-SER740
FGLN18-SER740
EGLN18-SER740

site_idSWS_FT_FI2
Number of Residues60
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354
ChainResidueDetails
DILE741-ILE761
FILE741-ILE761
EILE741-ILE761

site_idSWS_FT_FI3
Number of Residues129
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
DPHE762-PHE805
FPHE762-PHE805
EPHE762-PHE805

site_idSWS_FT_FI4
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
DGLU375
FGLU375
EGLU375

site_idSWS_FT_FI5
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
DHIS505
FHIS505
EHIS505

site_idSWS_FT_FI6
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
DARG169
BGLY1246
CTHR1238
CSER1239
CCYS1243
CLEU1244
CGLY1246
DTRP477
DLYS481
FARG169
FTRP477
FLYS481
EARG169
ETRP477
ELYS481

site_idSWS_FT_FI7
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
DARG273
BASP1257
CCYS1250
CGLY1251
CCYS1253
CPHE1256
CASP1257
DHIS345
DTYR515
FARG273
FHIS345
FTYR515
EARG273
EHIS345
ETYR515

site_idSWS_FT_FI8
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
DHIS374
DHIS378
DGLU402
FHIS374
FHIS378
FGLU402
EHIS374
EHIS378
EGLU402

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
DTYR781
BTHR1077
CTRP64
CASN125
CILE720
CGLN804
CTHR1077
FTYR781
ETYR781
AGLN804
ATHR1077
BTRP64
BASN125
BILE720
BGLN804

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
DSER783
FSER783
ESER783
BLYS77
BTRP152
BLEU1197
CLYS77
CTRP152
CLEU1197

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
DASN53
BASN334
BARG346
BGLU619
BTYR660
BHIS1101
CPHE168
CILE285
CASN334
CARG346
CGLU619
DASN322
CTYR660
CHIS1101
FASN53
FASN322
EASN53
EASN322
AHIS1101
BPHE168
BILE285

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
DASN90
FASN90
EASN90
BILE712
CARG237
CILE712

site_idSWS_FT_FI13
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
DASN103
DASN432
FASN103
FASN432
EASN103
EASN432

site_idSWS_FT_FI14
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
DASN546
FASN546
EASN546

site_idSWS_FT_FI15
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
DASN690
FASN690
EASN690

site_idSWS_FT_FI16
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523
ChainResidueDetails
DLYS788
AHIS681
FLYS788
BHIS681
ELYS788
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
AVAL1137
BVAL1137
CVAL1137

226707

PDB entries from 2024-10-30

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