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7XO7

SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with two 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
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
ETHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1444
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
EGLN18-SER740
FGLN18-SER740
CGLN17-ILE1216

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354
ChainResidueDetails
EILE741-ILE761
FILE741-ILE761
CTRP1217-MET1237

site_idSWS_FT_FI3
Number of Residues86
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
EPHE762-PHE805
FPHE762-PHE805

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
EGLU375
FGLU375
CALA688

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
EHIS505
FHIS505
CILE818

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
EARG169
BGLY1246
CTHR1238
CSER1239
CCYS1243
CLEU1244
CGLY1246
ETRP477
ELYS481
FARG169
FTRP477
FLYS481
BSER1239
BCYS1243
BLEU1244

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
EARG273
BASP1257
CCYS1250
CGLY1251
CCYS1253
CPHE1256
CASP1257
EHIS345
ETYR515
FARG273
FHIS345
FTYR515
BGLY1251
BCYS1253
BPHE1256

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
EHIS374
EHIS378
EGLU402
FHIS374
FHIS378
FGLU402
CASN20
CSER1161
CVAL1176

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
ETYR781
BTHR1077
CTRP64
CASN125
CILE720
CGLN804
CTHR1077
FTYR781
AILE720
AGLN804
ATHR1077
BTRP64
BASN125
BILE720
BGLN804

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
ESER783
FSER783
ALEU1197
BLYS77
BTRP152
BLEU1197
CLYS77
CTRP152
CLEU1197

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
EASN53
BASN334
BARG346
BGLU619
BTYR660
BHIS1101
CPHE168
CILE285
CASN334
CARG346
CGLU619
EASN322
CTYR660
CHIS1101
FASN53
FASN322
AGLU619
ATYR660
AHIS1101
BPHE168
BILE285

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
EASN90
FASN90
BARG237
BILE712
CARG237
CILE712

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
EASN103
EASN432
FASN103
FASN432

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
EASN546
FASN546
CARG328

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
EASN690
FASN690
CASN606

site_idSWS_FT_FI16
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523
ChainResidueDetails
ELYS788
AHIS681
FLYS788
BHIS681
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
AVAL1137
BVAL1137
CVAL1137

226707

PDB entries from 2024-10-30

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