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7EDJ

Cryo-EM structure of SARS-CoV-2 S-UK variant (B.1.1.7) in complex with Angiotensin-converting enzyme 2 (ACE2) ectodomain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019062biological_processvirion attachment to host cell
A0019064biological_processfusion of virus membrane with host plasma membrane
A0019065biological_processreceptor-mediated endocytosis of virus by host cell
A0019081biological_processviral translation
A0020002cellular_componenthost cell plasma membrane
A0039587biological_processsuppression by virus of host tetherin activity
A0039654biological_processfusion of virus membrane with host endosome membrane
A0039660molecular_functionstructural constituent of virion
A0042802molecular_functionidentical protein binding
A0043655cellular_componenthost extracellular space
A0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
A0044228cellular_componenthost cell surface
A0046598biological_processpositive regulation of viral entry into host cell
A0046718biological_processsymbiont entry into host cell
A0046789molecular_functionhost cell surface receptor binding
A0046813biological_processreceptor-mediated virion attachment to host cell
A0048018molecular_functionreceptor ligand activity
A0052170biological_processsymbiont-mediated suppression of host innate immune response
A0055036cellular_componentvirion membrane
A0061025biological_processmembrane fusion
A0075509biological_processendocytosis involved in viral entry into host cell
A0098670biological_processentry receptor-mediated virion attachment to host cell
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019062biological_processvirion attachment to host cell
B0019064biological_processfusion of virus membrane with host plasma membrane
B0019065biological_processreceptor-mediated endocytosis of virus by host cell
B0019081biological_processviral translation
B0020002cellular_componenthost cell plasma membrane
B0039587biological_processsuppression by virus of host tetherin activity
B0039654biological_processfusion of virus membrane with host endosome membrane
B0039660molecular_functionstructural constituent of virion
B0042802molecular_functionidentical protein binding
B0043655cellular_componenthost extracellular space
B0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
B0044228cellular_componenthost cell surface
B0046598biological_processpositive regulation of viral entry into host cell
B0046718biological_processsymbiont entry into host cell
B0046789molecular_functionhost cell surface receptor binding
B0046813biological_processreceptor-mediated virion attachment to host cell
B0048018molecular_functionreceptor ligand activity
B0052170biological_processsymbiont-mediated suppression of host innate immune response
B0055036cellular_componentvirion membrane
B0061025biological_processmembrane fusion
B0075509biological_processendocytosis involved in viral entry into host cell
B0098670biological_processentry receptor-mediated virion attachment to host cell
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019062biological_processvirion attachment to host cell
C0019064biological_processfusion of virus membrane with host plasma membrane
C0019065biological_processreceptor-mediated endocytosis of virus by host cell
C0019081biological_processviral translation
C0020002cellular_componenthost cell plasma membrane
C0039587biological_processsuppression by virus of host tetherin activity
C0039654biological_processfusion of virus membrane with host endosome membrane
C0039660molecular_functionstructural constituent of virion
C0042802molecular_functionidentical protein binding
C0043655cellular_componenthost extracellular space
C0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
C0044228cellular_componenthost cell surface
C0046598biological_processpositive regulation of viral entry into host cell
C0046718biological_processsymbiont entry into host cell
C0046789molecular_functionhost cell surface receptor binding
C0046813biological_processreceptor-mediated virion attachment to host cell
C0048018molecular_functionreceptor ligand activity
C0052170biological_processsymbiont-mediated suppression of host innate immune response
C0055036cellular_componentvirion membrane
C0061025biological_processmembrane fusion
C0075509biological_processendocytosis involved in viral entry into host cell
C0098670biological_processentry receptor-mediated virion attachment to host cell
I0003674molecular_functionmolecular_function
I0005575cellular_componentcellular_component
I0006091biological_processgeneration of precursor metabolites and energy
I0006508biological_processproteolysis
I0008218biological_processbioluminescence
I0008237molecular_functionmetallopeptidase activity
I0008241molecular_functionpeptidyl-dipeptidase activity
I0016020cellular_componentmembrane
J0003674molecular_functionmolecular_function
J0005575cellular_componentcellular_component
J0006091biological_processgeneration of precursor metabolites and energy
J0006508biological_processproteolysis
J0008218biological_processbioluminescence
J0008237molecular_functionmetallopeptidase activity
J0008241molecular_functionpeptidyl-dipeptidase activity
J0016020cellular_componentmembrane
K0003674molecular_functionmolecular_function
K0005575cellular_componentcellular_component
K0006091biological_processgeneration of precursor metabolites and energy
K0006508biological_processproteolysis
K0008218biological_processbioluminescence
K0008237molecular_functionmetallopeptidase activity
K0008241molecular_functionpeptidyl-dipeptidase activity
K0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ITHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
IGLU375
JGLU375
KGLU375

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
IHIS505
JHIS505
KHIS505

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
IARG169
ITRP477
ILYS481
JARG169
JTRP477
JLYS481
KARG169
KTRP477
KLYS481

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
IARG273
BTHR1074
CASN61
CTHR122
CILE717
CGLN801
CTHR1074
IHIS345
ITYR515
JARG273
JHIS345
JTYR515
KARG273
KHIS345
KTYR515

site_idSWS_FT_FI5
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
IHIS374
IHIS378
IGLU402
JHIS374
JHIS378
JGLU402
KHIS374
KHIS378
KGLU402

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
IASN53
BASN331
BARG343
BGLU616
BTYR657
BHIS1098
CPHE165
CILE282
CASN331
CARG343
CGLU616
IASN322
CTYR657
CHIS1098
JASN53
JASN322
KASN53
KASN322
AHIS1098
BPHE165
BILE282

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
IASN90
JASN90
KASN90
BILE709
CARG234
CILE709

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
IASN103
IASN432
JASN103
JASN432
KASN103
KASN432

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
IASN546
JASN546
KASN546

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
ITYR689
JTYR689
KTYR689

site_idSWS_FT_FI11
Number of Residues6
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
ITHR688
IGLY690
JTHR688
JGLY690
KTHR688
KGLY690

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
AVAL1134
BVAL1134
CVAL1134

223166

PDB entries from 2024-07-31

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