Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6U7F

HCoV-229E RBD Class IV in complex with human APN

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001618molecular_functionvirus receptor activity
A0002003biological_processangiotensin maturation
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005765cellular_componentlysosomal membrane
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009897cellular_componentexternal side of plasma membrane
A0016285molecular_functionalanyl aminopeptidase activity
A0016787molecular_functionhydrolase activity
A0030154biological_processcell differentiation
A0030667cellular_componentsecretory granule membrane
A0038023molecular_functionsignaling receptor activity
A0043171biological_processpeptide catabolic process
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
B0001525biological_processangiogenesis
B0001618molecular_functionvirus receptor activity
B0002003biological_processangiotensin maturation
B0004177molecular_functionaminopeptidase activity
B0005615cellular_componentextracellular space
B0005765cellular_componentlysosomal membrane
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0009897cellular_componentexternal side of plasma membrane
B0016285molecular_functionalanyl aminopeptidase activity
B0016787molecular_functionhydrolase activity
B0030154biological_processcell differentiation
B0030667cellular_componentsecretory granule membrane
B0038023molecular_functionsignaling receptor activity
B0043171biological_processpeptide catabolic process
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0070062cellular_componentextracellular exosome
C0019064biological_processfusion of virus membrane with host plasma membrane
D0019064biological_processfusion of virus membrane with host plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
AVAL385-TRP394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
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_FI2
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_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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_FI5
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
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_FI8
Number of Residues2
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_FI9
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon