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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7XID

S-ECD (Omicron) in complex with PD of ACE2

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019064biological_processfusion of virus membrane with host plasma membrane
A0039654biological_processfusion of virus membrane with host endosome membrane
A0046813biological_processreceptor-mediated virion attachment to host cell
A0055036cellular_componentvirion membrane
A0075509biological_processendocytosis involved in viral entry into host cell
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019064biological_processfusion of virus membrane with host plasma membrane
B0039654biological_processfusion of virus membrane with host endosome membrane
B0046813biological_processreceptor-mediated virion attachment to host cell
B0055036cellular_componentvirion membrane
B0075509biological_processendocytosis involved in viral entry into host cell
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019064biological_processfusion of virus membrane with host plasma membrane
C0039654biological_processfusion of virus membrane with host endosome membrane
C0046813biological_processreceptor-mediated virion attachment to host cell
C0055036cellular_componentvirion membrane
C0075509biological_processendocytosis involved in viral entry into host cell
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0001618molecular_functionvirus receptor activity
D0001817biological_processregulation of cytokine production
D0002003biological_processangiotensin maturation
D0003051biological_processangiotensin-mediated drinking behavior
D0003081biological_processregulation of systemic arterial blood pressure by renin-angiotensin
D0004175molecular_functionendopeptidase activity
D0004180molecular_functioncarboxypeptidase activity
D0004181molecular_functionmetallocarboxypeptidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005788cellular_componentendoplasmic reticulum lumen
D0005886cellular_componentplasma membrane
D0005929cellular_componentcilium
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0008241molecular_functionpeptidyl-dipeptidase activity
D0008270molecular_functionzinc ion binding
D0009986cellular_componentcell surface
D0015827biological_processtryptophan transport
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0016787molecular_functionhydrolase activity
D0019058biological_processviral life cycle
D0019065biological_processreceptor-mediated endocytosis of virus by host cell
D0019081biological_processviral translation
D0019229biological_processregulation of vasoconstriction
D0030666cellular_componentendocytic vesicle membrane
D0031526cellular_componentbrush border membrane
D0042127biological_processregulation of cell population proliferation
D0042802molecular_functionidentical protein binding
D0042995cellular_componentcell projection
D0045121cellular_componentmembrane raft
D0046513biological_processceramide biosynthetic process
D0046718biological_processsymbiont entry into host cell
D0046813biological_processreceptor-mediated virion attachment to host cell
D0046872molecular_functionmetal ion binding
D0048662biological_processnegative regulation of smooth muscle cell proliferation
D0050727biological_processregulation of inflammatory response
D0051957biological_processpositive regulation of amino acid transport
D0060135biological_processmaternal process involved in female pregnancy
D0060452biological_processpositive regulation of cardiac muscle contraction
D0061025biological_processmembrane fusion
D0070062cellular_componentextracellular exosome
D0070373biological_processnegative regulation of ERK1 and ERK2 cascade
D0097746biological_processblood vessel diameter maintenance
D0098670biological_processentry receptor-mediated virion attachment to host cell
D0141109molecular_functiontransporter activator activity
D1903598biological_processpositive regulation of gap junction assembly
D1903779biological_processregulation of cardiac conduction
D1905737biological_processpositive regulation of L-proline import across plasma membrane
D2000379biological_processpositive regulation of reactive oxygen species metabolic process
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0001618molecular_functionvirus receptor activity
E0001817biological_processregulation of cytokine production
E0002003biological_processangiotensin maturation
E0003051biological_processangiotensin-mediated drinking behavior
E0003081biological_processregulation of systemic arterial blood pressure by renin-angiotensin
E0004175molecular_functionendopeptidase activity
E0004180molecular_functioncarboxypeptidase activity
E0004181molecular_functionmetallocarboxypeptidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005737cellular_componentcytoplasm
E0005788cellular_componentendoplasmic reticulum lumen
E0005886cellular_componentplasma membrane
E0005929cellular_componentcilium
E0006508biological_processproteolysis
E0008233molecular_functionpeptidase activity
E0008237molecular_functionmetallopeptidase activity
E0008241molecular_functionpeptidyl-dipeptidase activity
E0008270molecular_functionzinc ion binding
E0009986cellular_componentcell surface
E0015827biological_processtryptophan transport
E0016020cellular_componentmembrane
E0016324cellular_componentapical plasma membrane
E0016787molecular_functionhydrolase activity
E0019058biological_processviral life cycle
E0019065biological_processreceptor-mediated endocytosis of virus by host cell
E0019081biological_processviral translation
E0019229biological_processregulation of vasoconstriction
E0030666cellular_componentendocytic vesicle membrane
E0031526cellular_componentbrush border membrane
E0042127biological_processregulation of cell population proliferation
E0042802molecular_functionidentical protein binding
E0042995cellular_componentcell projection
E0045121cellular_componentmembrane raft
E0046513biological_processceramide biosynthetic process
E0046718biological_processsymbiont entry into host cell
E0046813biological_processreceptor-mediated virion attachment to host cell
E0046872molecular_functionmetal ion binding
E0048662biological_processnegative regulation of smooth muscle cell proliferation
E0050727biological_processregulation of inflammatory response
E0051957biological_processpositive regulation of amino acid transport
E0060135biological_processmaternal process involved in female pregnancy
E0060452biological_processpositive regulation of cardiac muscle contraction
E0061025biological_processmembrane fusion
E0070062cellular_componentextracellular exosome
E0070373biological_processnegative regulation of ERK1 and ERK2 cascade
E0097746biological_processblood vessel diameter maintenance
E0098670biological_processentry receptor-mediated virion attachment to host cell
E0141109molecular_functiontransporter activator activity
E1903598biological_processpositive regulation of gap junction assembly
E1903779biological_processregulation of cardiac conduction
E1905737biological_processpositive regulation of L-proline import across plasma membrane
E2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
DTHR371-GLN380
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsRegion: {"description":"Putative superantigen; may bind T-cell receptor alpha/TRAC","evidences":[{"source":"PubMed","id":"32989130","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues184
DetailsRegion: {"description":"Disordered","evidences":[{"source":"PubMed","id":"35108439","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"Integrin-binding motif;","evidences":[{"source":"PubMed","id":"33102950","evidenceCode":"ECO:0000269"}]}
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; by host TMPRSS2 or CTSL","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32703818","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34159616","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues15
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (hybrid) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues21
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (HexNAc...) serine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (hybrid) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GlcNAc...) threonine; by host GALNT1","evidences":[{"source":"PubMed","id":"34732583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues386
DetailsDomain: {"description":"BetaCoV S1-CTD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01269","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32132184","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues444
DetailsRegion: {"description":"Receptor-binding domain (RBD)","evidences":[{"source":"PubMed","id":"32132184","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues142
DetailsRegion: {"description":"Receptor-binding motif; binding to human ACE2","evidences":[{"source":"UniProtKB","id":"P59594","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues16
DetailsRegion: {"description":"Immunodominant HLA epitope recognized by the CD8+; called NF9 peptide","evidences":[{"source":"PubMed","id":"34171266","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1176
DetailsDomain: {"description":"Peptidase M2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues34
DetailsRegion: {"description":"Interaction with SARS-CoV spike glycoprotein","evidences":[{"source":"PubMed","id":"15791205","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27217402","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19021774","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19901337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19901337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

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