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8YZD

Structure of JN.1 RBD protein 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
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008241molecular_functionpeptidyl-dipeptidase activity
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
BTHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
BGLU375

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
BHIS505

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
BARG169
BTRP477
BLYS481

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
BARG273
BHIS345
BTYR515
APRO809
ACYS1082

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
BHIS374
BHIS378
BGLU402

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
BASN53
BASN322
APHE338
AVAL350
AILE624
APRO665
AGLN1106

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
BASN90
AASN717

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
BASN103
BASN432

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
BASN546

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN690

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
AALA684
ASER686

site_idSWS_FT_FI12
Number of Residues1
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

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PDB entries from 2025-06-11

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