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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8WDE

CryoEM structure of the spike protein of human CoV 229E in complex with receptor hAPN (composite map)

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
D0001525biological_processangiogenesis
D0001618molecular_functionvirus receptor activity
D0002003biological_processangiotensin maturation
D0004177molecular_functionaminopeptidase activity
D0005615cellular_componentextracellular space
D0005765cellular_componentlysosomal membrane
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0009897cellular_componentexternal side of plasma membrane
D0016285molecular_functionalanyl aminopeptidase activity
D0016787molecular_functionhydrolase activity
D0030154biological_processcell differentiation
D0030667cellular_componentsecretory granule membrane
D0038023molecular_functionsignaling receptor activity
D0043171biological_processpeptide catabolic process
D0046718biological_processsymbiont entry into host cell
D0046872molecular_functionmetal ion binding
D0070006molecular_functionmetalloaminopeptidase activity
D0070062cellular_componentextracellular exosome
E0001525biological_processangiogenesis
E0001618molecular_functionvirus receptor activity
E0002003biological_processangiotensin maturation
E0004177molecular_functionaminopeptidase activity
E0005615cellular_componentextracellular space
E0005765cellular_componentlysosomal membrane
E0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
E0005886cellular_componentplasma membrane
E0006508biological_processproteolysis
E0008233molecular_functionpeptidase activity
E0008237molecular_functionmetallopeptidase activity
E0008270molecular_functionzinc ion binding
E0009897cellular_componentexternal side of plasma membrane
E0016285molecular_functionalanyl aminopeptidase activity
E0016787molecular_functionhydrolase activity
E0030154biological_processcell differentiation
E0030667cellular_componentsecretory granule membrane
E0038023molecular_functionsignaling receptor activity
E0043171biological_processpeptide catabolic process
E0046718biological_processsymbiont entry into host cell
E0046872molecular_functionmetal ion binding
E0070006molecular_functionmetalloaminopeptidase activity
E0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
DVAL385-TRP394
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues130
DetailsRegion: {"description":"Interaction with host ANPEP","evidences":[{"source":"HAMAP-Rule","id":"MF_04200","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues132
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04200","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"Necessary and sufficient to mediate interaction with HCoV-229E","evidences":[{"source":"PubMed","id":"1350662","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8887485","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FYQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FYR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FYT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

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PDB entries from 2026-01-21

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