Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6VSJ

Cryo-electron microscopy structure of mouse coronavirus spike protein complexed with its murine receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003700molecular_functionDNA-binding transcription factor activity
A0005515molecular_functionprotein binding
A0006355biological_processregulation of DNA-templated transcription
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
A0042802molecular_functionidentical protein binding
A0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
A0044177cellular_componenthost cell Golgi apparatus
A0046718biological_processsymbiont entry into host cell
A0046813biological_processreceptor-mediated virion attachment to host cell
A0055036cellular_componentvirion membrane
A0075509biological_processendocytosis involved in viral entry into host cell
B0003700molecular_functionDNA-binding transcription factor activity
B0005515molecular_functionprotein binding
B0006355biological_processregulation of DNA-templated transcription
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
B0042802molecular_functionidentical protein binding
B0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
B0044177cellular_componenthost cell Golgi apparatus
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0055036cellular_componentvirion membrane
B0075509biological_processendocytosis involved in viral entry into host cell
C0003700molecular_functionDNA-binding transcription factor activity
C0005515molecular_functionprotein binding
C0006355biological_processregulation of DNA-templated transcription
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
C0042802molecular_functionidentical protein binding
C0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
C0044177cellular_componenthost cell Golgi apparatus
C0046718biological_processsymbiont entry into host cell
C0046813biological_processreceptor-mediated virion attachment to host cell
C0055036cellular_componentvirion membrane
C0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:11980704, ECO:0000269|PubMed:19349973
ChainResidueDetails
DASN71
DASN89
EASN71
EASN89
FASN71
FASN89

site_idSWS_FT_FI2
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:11980704
ChainResidueDetails
DASN104
EASN104
FASN104

site_idSWS_FT_FI3
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
DPHE148
AASN688
AASN737
AASN754
AASN893
AASN1180
AASN1190
AASN1209
AASN1225
BASN31
BASN60
DLEU199
BASN192
BASN357
BASN435
BASN530
BASN625
BASN657
BASN665
BASN688
BASN737
BASN754
EPHE148
BASN893
BASN1180
BASN1190
BASN1209
BASN1225
CASN31
CASN60
CASN192
CASN357
CASN435
ELEU199
CASN530
CASN625
CASN657
CASN665
CASN688
CASN737
CASN754
CASN893
CASN1180
CASN1190
FPHE148
CASN1209
CASN1225
FLEU199
AASN625
AASN657
AASN665

site_idSWS_FT_FI4
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P13688, ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
DTHR152
DGLY210
DASN226
ETHR152
EGLY210
EASN226
FTHR152
FGLY210
FASN226

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:16944957
ChainResidueDetails
DARG206
EARG206
FARG206

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon