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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8ZE6

Crystal structure of MjHKU4r-CoV-1 RBD bound to MjDPP4

Functional Information from GO Data
ChainGOidnamespacecontents
B0001618molecular_functionvirus receptor activity
B0001666biological_processresponse to hypoxia
B0002020molecular_functionprotease binding
B0004177molecular_functionaminopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006508biological_processproteolysis
B0007155biological_processcell adhesion
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0008284biological_processpositive regulation of cell population proliferation
B0009986cellular_componentcell surface
B0010716biological_processnegative regulation of extracellular matrix disassembly
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016486biological_processpeptide hormone processing
B0016787molecular_functionhydrolase activity
B0019065biological_processreceptor-mediated endocytosis of virus by host cell
B0030027cellular_componentlamellipodium
B0030139cellular_componentendocytic vesicle
B0031258cellular_componentlamellipodium membrane
B0031295biological_processT cell costimulation
B0033632biological_processregulation of cell-cell adhesion mediated by integrin
B0042110biological_processT cell activation
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042995cellular_componentcell projection
B0043542biological_processendothelial cell migration
B0045121cellular_componentmembrane raft
B0045499molecular_functionchemorepellent activity
B0046581cellular_componentintercellular canaliculus
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0050919biological_processnegative chemotaxis
B0061025biological_processmembrane fusion
B0070062cellular_componentextracellular exosome
B0070161cellular_componentanchoring junction
B0090024biological_processnegative regulation of neutrophil chemotaxis
B0120116biological_processglucagon processing
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
Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFtnmgfvdekriaiwGwSyGGYV
ChainResidueDetails
BASP605-VAL635
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_FI3
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_FI4
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_FI5
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_FI6
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_FI7
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_FI8
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_FI9
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
site_idMCSA2
Number of Residues5
DetailsM-CSA 169
ChainResidueDetails

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PDB entries from 2025-12-03

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