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7V85

Cryo-EM structure of SARS-CoV-2 S-Kappa variant (B.1.617.1) in complex with Angiotensin-converting enzyme 2 (ACE2) ectodomain, two ACE2-bound form

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
F0006091biological_processgeneration of precursor metabolites and energy
F0006508biological_processproteolysis
F0008218biological_processbioluminescence
F0008237molecular_functionmetallopeptidase activity
F0008241molecular_functionpeptidyl-dipeptidase activity
F0016020cellular_componentmembrane
H0006091biological_processgeneration of precursor metabolites and energy
H0006508biological_processproteolysis
H0008218biological_processbioluminescence
H0008237molecular_functionmetallopeptidase activity
H0008241molecular_functionpeptidyl-dipeptidase activity
H0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
FTHR371-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
FGLU375
HGLU375
CSER685

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
FHIS505
HHIS505
CARG815

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
FARG169
FTRP477
FLYS481
HARG169
HTRP477
HLYS481
CASN17
CASN1158
CASN1173

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
FARG273
BASN1074
CASN61
CASN122
CASN717
CASN801
CASN1074
FHIS345
FTYR515
HARG273
HHIS345
HTYR515
BASN122
BASN717
BASN801

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
FHIS374
FHIS378
FGLU402
HHIS374
HHIS378
HGLU402
CASN74
CASN149
CASN1194

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
FASN53
BASN331
BASN343
BASN616
BASN657
BASN1098
CASN165
CASN282
CASN331
CASN343
CASN616
FASN322
CASN657
CASN1098
HASN53
HASN322
AASN616
AASN657
AASN1098
BASN165
BASN282

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
FASN90
HASN90
BASN234
BASN709
CASN234
CASN709

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
FASN103
FASN432
HASN103
HASN432

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
FASN546
HASN546
CSER325

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
AASN603
BASN603
CASN603

site_idSWS_FT_FI11
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_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

218853

PDB entries from 2024-04-24

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