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7CT5

S protein of SARS-CoV-2 in complex bound with T-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
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 Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
DGLU375
EGLU375
FGLU375

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
DHIS505
EHIS505
FHIS505

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
DARG169
DTRP477
DLYS481
EARG169
ETRP477
ELYS481
FARG169
FTRP477
FLYS481

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
DARG273
DHIS345
DTYR515
EARG273
EHIS345
ETYR515
FARG273
FHIS345
FTYR515

site_idSWS_FT_FI5
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
DHIS374
DHIS378
DGLU402
EHIS374
EHIS378
EGLU402
FHIS374
FHIS378
FGLU402

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
DASN53
BCYS1243
CCYS1235
CCYS1236
CCYS1240
CCYS1241
CCYS1243
DASN322
EASN53
EASN322
FASN53
FASN322
BCYS1236
BCYS1240
BCYS1241

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
DASN90
BCYS1254
CCYS1247
CCYS1248
CCYS1250
CCYS1253
CCYS1254
EASN90
FASN90
ACYS1253
ACYS1254
BCYS1247
BCYS1248
BCYS1250
BCYS1253

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
DASN103
DASN432
EASN103
EASN432
FASN103
FASN432
CASN17
CASN1158
CASN1173

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
DASN546
BASN1074
CASN61
CASN122
CASN717
CASN801
CASN1074
EASN546
FASN546
AASN801
AASN1074
BASN61
BASN122
BASN717
BASN801

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
AASN74
AASN149
AASN1194
BASN74
BASN149
BASN1194
CASN74
CASN149
CASN1194

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
AASN165
BASN331
BASN343
BASN616
BASN657
BASN1098
CASN165
CASN282
CASN331
CASN343
CASN616
AASN282
CASN657
CASN1098
AASN331
AASN343
AASN616
AASN657
AASN1098
BASN165
BASN282

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
AASN234
AASN709
BASN234
BASN709
CASN234
CASN709

site_idSWS_FT_FI13
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ATHR323
BTHR323
CTHR323

site_idSWS_FT_FI14
Number of Residues3
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ASER325
BSER325
CSER325

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
AASN603
BASN603
CASN603

site_idSWS_FT_FI16
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
ATHR676
ATHR678
BTHR676
BTHR678
CTHR676
CTHR678

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
AASN1134
BASN1134
CASN1134

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PDB entries from 2024-05-08

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