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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8Z4T

MERS-CoV S ectodomain trimer in complex with receptor DPP4-750E

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019062biological_processvirion attachment to host cell
A0019064biological_processfusion of virus membrane with host plasma membrane
A0020002cellular_componenthost cell plasma membrane
A0039654biological_processfusion of virus membrane with host endosome membrane
A0039663biological_processmembrane fusion involved in viral entry into host cell
A0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
A0044423cellular_componentvirion component
A0046598biological_processpositive regulation of viral entry into host cell
A0046718biological_processsymbiont entry into host cell
A0046813biological_processreceptor-mediated virion attachment to host cell
A0055036cellular_componentvirion membrane
A0061025biological_processmembrane fusion
A0075509biological_processendocytosis involved in viral entry into host cell
B0005515molecular_functionprotein binding
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019062biological_processvirion attachment to host cell
B0019064biological_processfusion of virus membrane with host plasma membrane
B0020002cellular_componenthost cell plasma membrane
B0039654biological_processfusion of virus membrane with host endosome membrane
B0039663biological_processmembrane fusion involved in viral entry into host cell
B0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
B0044423cellular_componentvirion component
B0046598biological_processpositive regulation of viral entry into host cell
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0055036cellular_componentvirion membrane
B0061025biological_processmembrane fusion
B0075509biological_processendocytosis involved in viral entry into host cell
C0005515molecular_functionprotein binding
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019062biological_processvirion attachment to host cell
C0019064biological_processfusion of virus membrane with host plasma membrane
C0020002cellular_componenthost cell plasma membrane
C0039654biological_processfusion of virus membrane with host endosome membrane
C0039663biological_processmembrane fusion involved in viral entry into host cell
C0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
C0044423cellular_componentvirion component
C0046598biological_processpositive regulation of viral entry into host cell
C0046718biological_processsymbiont entry into host cell
C0046813biological_processreceptor-mediated virion attachment to host cell
C0055036cellular_componentvirion membrane
C0061025biological_processmembrane fusion
C0075509biological_processendocytosis involved in viral entry into host cell
D0001618molecular_functionvirus receptor activity
D0001666biological_processresponse to hypoxia
D0002020molecular_functionprotease binding
D0004177molecular_functionaminopeptidase activity
D0004252molecular_functionserine-type endopeptidase activity
D0005102molecular_functionsignaling receptor binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005765cellular_componentlysosomal membrane
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006508biological_processproteolysis
D0007155biological_processcell adhesion
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0008239molecular_functiondipeptidyl-peptidase activity
D0008284biological_processpositive regulation of cell population proliferation
D0009986cellular_componentcell surface
D0010716biological_processnegative regulation of extracellular matrix disassembly
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0016486biological_processpeptide hormone processing
D0016787molecular_functionhydrolase activity
D0019065biological_processreceptor-mediated endocytosis of virus by host cell
D0030027cellular_componentlamellipodium
D0030139cellular_componentendocytic vesicle
D0031258cellular_componentlamellipodium membrane
D0031295biological_processT cell costimulation
D0033632biological_processregulation of cell-cell adhesion mediated by integrin
D0042110biological_processT cell activation
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0042995cellular_componentcell projection
D0043542biological_processendothelial cell migration
D0045121cellular_componentmembrane raft
D0045499molecular_functionchemorepellent activity
D0046581cellular_componentintercellular canaliculus
D0046718biological_processsymbiont entry into host cell
D0046813biological_processreceptor-mediated virion attachment to host cell
D0050919biological_processnegative chemotaxis
D0061025biological_processmembrane fusion
D0070062cellular_componentextracellular exosome
D0070161cellular_componentanchoring junction
D0090024biological_processnegative regulation of neutrophil chemotaxis
D0120116biological_processglucagon processing
I0001618molecular_functionvirus receptor activity
I0001666biological_processresponse to hypoxia
I0002020molecular_functionprotease binding
I0004177molecular_functionaminopeptidase activity
I0004252molecular_functionserine-type endopeptidase activity
I0005102molecular_functionsignaling receptor binding
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005765cellular_componentlysosomal membrane
I0005886cellular_componentplasma membrane
I0005925cellular_componentfocal adhesion
I0006508biological_processproteolysis
I0007155biological_processcell adhesion
I0008233molecular_functionpeptidase activity
I0008236molecular_functionserine-type peptidase activity
I0008239molecular_functiondipeptidyl-peptidase activity
I0008284biological_processpositive regulation of cell population proliferation
I0009986cellular_componentcell surface
I0010716biological_processnegative regulation of extracellular matrix disassembly
I0016020cellular_componentmembrane
I0016324cellular_componentapical plasma membrane
I0016486biological_processpeptide hormone processing
I0016787molecular_functionhydrolase activity
I0019065biological_processreceptor-mediated endocytosis of virus by host cell
I0030027cellular_componentlamellipodium
I0030139cellular_componentendocytic vesicle
I0031258cellular_componentlamellipodium membrane
I0031295biological_processT cell costimulation
I0033632biological_processregulation of cell-cell adhesion mediated by integrin
I0042110biological_processT cell activation
I0042802molecular_functionidentical protein binding
I0042803molecular_functionprotein homodimerization activity
I0042995cellular_componentcell projection
I0043542biological_processendothelial cell migration
I0045121cellular_componentmembrane raft
I0045499molecular_functionchemorepellent activity
I0046581cellular_componentintercellular canaliculus
I0046718biological_processsymbiont entry into host cell
I0046813biological_processreceptor-mediated virion attachment to host cell
I0050919biological_processnegative chemotaxis
I0061025biological_processmembrane fusion
I0070062cellular_componentextracellular exosome
I0070161cellular_componentanchoring junction
I0090024biological_processnegative regulation of neutrophil chemotaxis
I0120116biological_processglucagon processing
Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
ChainResidueDetails
DASP605-VAL635
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsRegion: {"description":"Fusion peptide 1","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues66
DetailsRegion: {"description":"Fusion peptide 2","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues150
DetailsRegion: {"description":"Heptad repeat 1","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues132
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Cleavage","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues46
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12483204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20684603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23835475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails
DTYR547electrostatic stabiliser, hydrogen bond donor
DSER630covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
DTYR631electrostatic stabiliser, hydrogen bond donor
DASP708activator, electrostatic stabiliser, hydrogen bond acceptor
DHIS740electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
site_idMCSA2
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails

250059

PDB entries from 2026-03-04

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