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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7DWX

Conformation 1 of S-ACE2-B0AT1 ternary complex

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006836biological_processneurotransmitter transport
A0006865biological_processamino acid transport
A0007584biological_processresponse to nutrient
A0015171molecular_functionamino acid transmembrane transporter activity
A0015175molecular_functionneutral L-amino acid transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015804biological_processneutral amino acid transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0019058biological_processviral life cycle
A0022857molecular_functiontransmembrane transporter activity
A0031526cellular_componentbrush border membrane
A0035725biological_processsodium ion transmembrane transport
A0070062cellular_componentextracellular exosome
A0089718biological_processamino acid import across plasma membrane
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001618molecular_functionvirus receptor activity
B0001817biological_processregulation of cytokine production
B0002003biological_processangiotensin maturation
B0003051biological_processangiotensin-mediated drinking behavior
B0003081biological_processregulation of systemic arterial blood pressure by renin-angiotensin
B0004175molecular_functionendopeptidase activity
B0004180molecular_functioncarboxypeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005788cellular_componentendoplasmic reticulum lumen
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008241molecular_functionpeptidyl-dipeptidase activity
B0008270molecular_functionzinc ion binding
B0009986cellular_componentcell surface
B0015827biological_processtryptophan transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016787molecular_functionhydrolase activity
B0019058biological_processviral life cycle
B0019065biological_processreceptor-mediated endocytosis of virus by host cell
B0019229biological_processregulation of vasoconstriction
B0030666cellular_componentendocytic vesicle membrane
B0031526cellular_componentbrush border membrane
B0042127biological_processregulation of cell population proliferation
B0042802molecular_functionidentical protein binding
B0045121cellular_componentmembrane raft
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0046872molecular_functionmetal ion binding
B0048662biological_processnegative regulation of smooth muscle cell proliferation
B0050727biological_processregulation of inflammatory response
B0051957biological_processpositive regulation of amino acid transport
B0060135biological_processmaternal process involved in female pregnancy
B0060452biological_processpositive regulation of cardiac muscle contraction
B0061025biological_processmembrane fusion
B0070062cellular_componentextracellular exosome
B0070373biological_processnegative regulation of ERK1 and ERK2 cascade
B0089718biological_processamino acid import across plasma membrane
B0097746biological_processblood vessel diameter maintenance
B0098670biological_processentry receptor-mediated virion attachment to host cell
B0141109molecular_functiontransporter activator activity
B1903598biological_processpositive regulation of gap junction assembly
B1903779biological_processregulation of cardiac conduction
B1905737biological_processpositive regulation of L-proline import across plasma membrane
B2000379biological_processpositive regulation of reactive oxygen species metabolic process
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0006836biological_processneurotransmitter transport
C0006865biological_processamino acid transport
C0007584biological_processresponse to nutrient
C0015171molecular_functionamino acid transmembrane transporter activity
C0015175molecular_functionneutral L-amino acid transmembrane transporter activity
C0015293molecular_functionsymporter activity
C0015804biological_processneutral amino acid transport
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0019058biological_processviral life cycle
C0022857molecular_functiontransmembrane transporter activity
C0031526cellular_componentbrush border membrane
C0035725biological_processsodium ion transmembrane transport
C0070062cellular_componentextracellular exosome
C0089718biological_processamino acid import across plasma membrane
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
D0019229biological_processregulation of vasoconstriction
D0030666cellular_componentendocytic vesicle membrane
D0031526cellular_componentbrush border membrane
D0042127biological_processregulation of cell population proliferation
D0042802molecular_functionidentical protein binding
D0045121cellular_componentmembrane raft
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
D0089718biological_processamino acid import across plasma membrane
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
E0016020cellular_componentmembrane
E0019031cellular_componentviral envelope
E0019064biological_processfusion of virus membrane with host plasma membrane
E0039654biological_processfusion of virus membrane with host endosome membrane
E0046813biological_processreceptor-mediated virion attachment to host cell
E0055036cellular_componentvirion membrane
E0075509biological_processendocytosis involved in viral entry into host cell
F0016020cellular_componentmembrane
F0019031cellular_componentviral envelope
F0019064biological_processfusion of virus membrane with host plasma membrane
F0039654biological_processfusion of virus membrane with host endosome membrane
F0046813biological_processreceptor-mediated virion attachment to host cell
F0055036cellular_componentvirion membrane
F0075509biological_processendocytosis involved in viral entry into host cell
G0016020cellular_componentmembrane
G0019031cellular_componentviral envelope
G0019064biological_processfusion of virus membrane with host plasma membrane
G0039654biological_processfusion of virus membrane with host endosome membrane
G0046813biological_processreceptor-mediated virion attachment to host cell
G0055036cellular_componentvirion membrane
G0075509biological_processendocytosis involved in viral entry into host cell
H0016020cellular_componentmembrane
H0019031cellular_componentviral envelope
H0019064biological_processfusion of virus membrane with host plasma membrane
H0039654biological_processfusion of virus membrane with host endosome membrane
H0046813biological_processreceptor-mediated virion attachment to host cell
H0055036cellular_componentvirion membrane
H0075509biological_processendocytosis involved in viral entry into host cell
I0016020cellular_componentmembrane
I0019031cellular_componentviral envelope
I0019064biological_processfusion of virus membrane with host plasma membrane
I0039654biological_processfusion of virus membrane with host endosome membrane
I0046813biological_processreceptor-mediated virion attachment to host cell
I0055036cellular_componentvirion membrane
I0075509biological_processendocytosis involved in viral entry into host cell
J0016020cellular_componentmembrane
J0019031cellular_componentviral envelope
J0019064biological_processfusion of virus membrane with host plasma membrane
J0039654biological_processfusion of virus membrane with host endosome membrane
J0046813biological_processreceptor-mediated virion attachment to host cell
J0055036cellular_componentvirion membrane
J0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
BTHR371-GLN380
site_idPS00610
Number of Residues15
DetailsNA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcqsHGGGaF
ChainResidueDetails
ATRP56-PHE70
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues412
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues184
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9D687","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01354","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues34
DetailsRegion: {"description":"Interaction with SARS-CoV spike glycoprotein","evidences":[{"source":"PubMed","id":"15791205","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues14
DetailsRegion: {"description":"Essential for cleavage by ADAM17","evidences":[{"source":"PubMed","id":"24227843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues38
DetailsRegion: {"description":"Essential for cleavage by TMPRSS11D and TMPRSS2","evidences":[{"source":"PubMed","id":"24227843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
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_FI22
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_FI23
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_FI24
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI25
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_FI26
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI27
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_FI28
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
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
site_idSWS_FT_FI30
Number of Residues1158
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_FI31
Number of Residues126
DetailsRegion: {"description":"Putative superantigen; may bind T-cell receptor alpha/TRAC","evidences":[{"source":"PubMed","id":"32989130","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1332
DetailsRegion: {"description":"Receptor-binding domain (RBD)","evidences":[{"source":"PubMed","id":"32132184","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues438
DetailsRegion: {"description":"Disordered","evidences":[{"source":"PubMed","id":"35108439","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues12
DetailsRegion: {"description":"Integrin-binding motif;","evidences":[{"source":"PubMed","id":"33102950","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues426
DetailsRegion: {"description":"Receptor-binding motif; binding to human ACE2","evidences":[{"source":"UniProtKB","id":"P59594","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues48
DetailsRegion: {"description":"Immunodominant HLA epitope recognized by the CD8+; called NF9 peptide","evidences":[{"source":"PubMed","id":"34171266","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues264
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues6
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_FI39
Number of Residues30
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_FI40
Number of Residues42
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_FI41
Number of Residues12
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_FI42
Number of Residues6
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues6
DetailsGlycosylation: {"description":"O-linked (HexNAc...) serine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues6
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_FI45
Number of Residues6
DetailsGlycosylation: {"description":"O-linked (GlcNAc...) threonine; by host GALNT1","evidences":[{"source":"PubMed","id":"34732583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues6
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

246704

PDB entries from 2025-12-24

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