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8YZE

The JN.1 spike protein (S) in complex with ACE2.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019062biological_processvirion attachment to host cell
A0019064biological_processfusion of virus membrane with host plasma membrane
A0019081biological_processviral translation
A0020002cellular_componenthost cell plasma membrane
A0033644cellular_componenthost cell membrane
A0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
A0039654biological_processfusion of virus membrane with host endosome membrane
A0039660molecular_functionstructural constituent of virion
A0039663biological_processmembrane fusion involved in viral entry into host cell
A0042802molecular_functionidentical protein binding
A0043655cellular_componenthost extracellular space
A0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
A0044228cellular_componenthost cell surface
A0044423cellular_componentvirion component
A0046598biological_processpositive regulation of viral entry into host cell
A0046718biological_processsymbiont entry into host cell
A0046789molecular_functionhost cell surface receptor binding
A0046813biological_processreceptor-mediated virion attachment to host cell
A0048018molecular_functionreceptor ligand activity
A0052170biological_processsymbiont-mediated suppression of host innate immune response
A0055036cellular_componentvirion membrane
A0061025biological_processmembrane fusion
A0075509biological_processendocytosis involved in viral entry into host cell
A0098670biological_processentry receptor-mediated virion attachment to host cell
A0141146biological_processsymbiont-mediated disruption of host tissue
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019062biological_processvirion attachment to host cell
B0019064biological_processfusion of virus membrane with host plasma membrane
B0019081biological_processviral translation
B0020002cellular_componenthost cell plasma membrane
B0033644cellular_componenthost cell membrane
B0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
B0039654biological_processfusion of virus membrane with host endosome membrane
B0039660molecular_functionstructural constituent of virion
B0039663biological_processmembrane fusion involved in viral entry into host cell
B0042802molecular_functionidentical protein binding
B0043655cellular_componenthost extracellular space
B0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
B0044228cellular_componenthost cell surface
B0044423cellular_componentvirion component
B0046598biological_processpositive regulation of viral entry into host cell
B0046718biological_processsymbiont entry into host cell
B0046789molecular_functionhost cell surface receptor binding
B0046813biological_processreceptor-mediated virion attachment to host cell
B0048018molecular_functionreceptor ligand activity
B0052170biological_processsymbiont-mediated suppression of host innate immune response
B0055036cellular_componentvirion membrane
B0061025biological_processmembrane fusion
B0075509biological_processendocytosis involved in viral entry into host cell
B0098670biological_processentry receptor-mediated virion attachment to host cell
B0141146biological_processsymbiont-mediated disruption of host tissue
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019062biological_processvirion attachment to host cell
C0019064biological_processfusion of virus membrane with host plasma membrane
C0019081biological_processviral translation
C0020002cellular_componenthost cell plasma membrane
C0033644cellular_componenthost cell membrane
C0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
C0039654biological_processfusion of virus membrane with host endosome membrane
C0039660molecular_functionstructural constituent of virion
C0039663biological_processmembrane fusion involved in viral entry into host cell
C0042802molecular_functionidentical protein binding
C0043655cellular_componenthost extracellular space
C0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
C0044228cellular_componenthost cell surface
C0044423cellular_componentvirion component
C0046598biological_processpositive regulation of viral entry into host cell
C0046718biological_processsymbiont entry into host cell
C0046789molecular_functionhost cell surface receptor binding
C0046813biological_processreceptor-mediated virion attachment to host cell
C0048018molecular_functionreceptor ligand activity
C0052170biological_processsymbiont-mediated suppression of host innate immune response
C0055036cellular_componentvirion membrane
C0061025biological_processmembrane fusion
C0075509biological_processendocytosis involved in viral entry into host cell
C0098670biological_processentry receptor-mediated virion attachment to host cell
C0141146biological_processsymbiont-mediated disruption of host tissue
G0006508biological_processproteolysis
G0008237molecular_functionmetallopeptidase activity
G0008241molecular_functionpeptidyl-dipeptidase activity
G0016020cellular_componentmembrane
H0006508biological_processproteolysis
H0008237molecular_functionmetallopeptidase activity
H0008241molecular_functionpeptidyl-dipeptidase activity
H0016020cellular_componentmembrane
I0006508biological_processproteolysis
I0008237molecular_functionmetallopeptidase activity
I0008241molecular_functionpeptidyl-dipeptidase activity
I0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
GTHR371-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
GGLU375
HGLU375
IGLU375

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
GHIS505
HHIS505
IHIS505

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
GARG169
GTRP477
GLYS481
HARG169
HTRP477
HLYS481
IARG169
ITRP477
ILYS481

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
GARG273
BCYS1082
CTRP68
CVAL129
CGLU725
CPRO809
CCYS1082
GHIS345
GTYR515
HARG273
HHIS345
HTYR515
IARG273
IHIS345
ITYR515

site_idSWS_FT_FI5
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
GHIS374
GHIS378
GGLU402
HHIS374
HHIS378
HGLU402
IHIS374
IHIS378
IGLU402

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
GASN53
BPHE338
BVAL350
BILE624
BPRO665
BGLN1106
CVAL172
CVAL289
CPHE338
CVAL350
CILE624
GASN322
CPRO665
CGLN1106
HASN53
HASN322
IASN53
IASN322
AGLN1106
BVAL172
BVAL289

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
GASN90
HASN90
IASN90
BASN717
CLEU241
CASN717

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
GASN103
GASN432
HASN103
HASN432
IASN103
IASN432

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
GASN546
HASN546
IASN546

site_idSWS_FT_FI10
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
GASN690
HASN690
IASN690

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
AALA684
ASER686
BALA684
BSER686
CALA684
CSER686

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
AGLN1142
BGLN1142
CGLN1142

237992

PDB entries from 2025-06-25

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