Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9RGE

CryoEM structure of human alpha1beta3gamma2 GABA(A)R in complex with GARLH4 and the Neuroligin2 transmembrane helix, in CL47a

Functional Information from GO Data
ChainGOidnamespacecontents
A0004890molecular_functionGABA-A receptor activity
A0005886cellular_componentplasma membrane
A0007214biological_processgamma-aminobutyric acid signaling pathway
A0016917molecular_functionGABA receptor activity
A0022851molecular_functionGABA-gated chloride ion channel activity
A0030659cellular_componentcytoplasmic vesicle membrane
A0032590cellular_componentdendrite membrane
A0038023molecular_functionsignaling receptor activity
A0043197cellular_componentdendritic spine
A0045211cellular_componentpostsynaptic membrane
A0051932biological_processsynaptic transmission, GABAergic
A0060078biological_processregulation of postsynaptic membrane potential
A0098794cellular_componentpostsynapse
A0098982cellular_componentGABA-ergic synapse
A0099634cellular_componentpostsynaptic specialization membrane
A0160001biological_processextrasynaptic signaling via GABA
A1902476biological_processchloride transmembrane transport
A1902710cellular_componentGABA receptor complex
A1902711cellular_componentGABA-A receptor complex
A1904315molecular_functiontransmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential
A1904862biological_processinhibitory synapse assembly
B0004890molecular_functionGABA-A receptor activity
B0005102molecular_functionsignaling receptor binding
B0005216molecular_functionmonoatomic ion channel activity
B0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
B0005254molecular_functionchloride channel activity
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007214biological_processgamma-aminobutyric acid signaling pathway
B0007268biological_processchemical synaptic transmission
B0009986cellular_componentcell surface
B0022851molecular_functionGABA-gated chloride ion channel activity
B0030659cellular_componentcytoplasmic vesicle membrane
B0032229biological_processnegative regulation of synaptic transmission, GABAergic
B0034707cellular_componentchloride channel complex
B0042802molecular_functionidentical protein binding
B0043197cellular_componentdendritic spine
B0045202cellular_componentsynapse
B0045211cellular_componentpostsynaptic membrane
B0048666biological_processneuron development
B0051932biological_processsynaptic transmission, GABAergic
B0060021biological_processroof of mouth development
B0060080biological_processinhibitory postsynaptic potential
B0060119biological_processinner ear receptor cell development
B0060384biological_processinnervation
B0071420biological_processcellular response to histamine
B0071514biological_processgenomic imprinting
B0090102biological_processcochlea development
B0098982cellular_componentGABA-ergic synapse
B0099634cellular_componentpostsynaptic specialization membrane
B0160001biological_processextrasynaptic signaling via GABA
B1902476biological_processchloride transmembrane transport
B1902711cellular_componentGABA-A receptor complex
B1904315molecular_functiontransmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential
B1904862biological_processinhibitory synapse assembly
C0004890molecular_functionGABA-A receptor activity
C0005254molecular_functionchloride channel activity
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0007214biological_processgamma-aminobutyric acid signaling pathway
C0008503molecular_functionbenzodiazepine receptor activity
C0022851molecular_functionGABA-gated chloride ion channel activity
C0030424cellular_componentaxon
C0030425cellular_componentdendrite
C0030659cellular_componentcytoplasmic vesicle membrane
C0032229biological_processnegative regulation of synaptic transmission, GABAergic
C0032590cellular_componentdendrite membrane
C0034707cellular_componentchloride channel complex
C0045211cellular_componentpostsynaptic membrane
C0051932biological_processsynaptic transmission, GABAergic
C0060078biological_processregulation of postsynaptic membrane potential
C0071420biological_processcellular response to histamine
C0098794cellular_componentpostsynapse
C0098982cellular_componentGABA-ergic synapse
C0099634cellular_componentpostsynaptic specialization membrane
C0160001biological_processextrasynaptic signaling via GABA
C1902476biological_processchloride transmembrane transport
C1902711cellular_componentGABA-A receptor complex
C1904315molecular_functiontransmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential
C1904862biological_processinhibitory synapse assembly
D0004890molecular_functionGABA-A receptor activity
D0005886cellular_componentplasma membrane
D0007214biological_processgamma-aminobutyric acid signaling pathway
D0016917molecular_functionGABA receptor activity
D0022851molecular_functionGABA-gated chloride ion channel activity
D0030659cellular_componentcytoplasmic vesicle membrane
D0032590cellular_componentdendrite membrane
D0038023molecular_functionsignaling receptor activity
D0043197cellular_componentdendritic spine
D0045211cellular_componentpostsynaptic membrane
D0051932biological_processsynaptic transmission, GABAergic
D0060078biological_processregulation of postsynaptic membrane potential
D0098794cellular_componentpostsynapse
D0098982cellular_componentGABA-ergic synapse
D0099634cellular_componentpostsynaptic specialization membrane
D0160001biological_processextrasynaptic signaling via GABA
D1902476biological_processchloride transmembrane transport
D1902710cellular_componentGABA receptor complex
D1902711cellular_componentGABA-A receptor complex
D1904315molecular_functiontransmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential
D1904862biological_processinhibitory synapse assembly
E0004890molecular_functionGABA-A receptor activity
E0005102molecular_functionsignaling receptor binding
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0005254molecular_functionchloride channel activity
E0005886cellular_componentplasma membrane
E0007165biological_processsignal transduction
E0007214biological_processgamma-aminobutyric acid signaling pathway
E0007268biological_processchemical synaptic transmission
E0009986cellular_componentcell surface
E0022851molecular_functionGABA-gated chloride ion channel activity
E0030659cellular_componentcytoplasmic vesicle membrane
E0032229biological_processnegative regulation of synaptic transmission, GABAergic
E0034707cellular_componentchloride channel complex
E0042802molecular_functionidentical protein binding
E0043197cellular_componentdendritic spine
E0045202cellular_componentsynapse
E0045211cellular_componentpostsynaptic membrane
E0048666biological_processneuron development
E0051932biological_processsynaptic transmission, GABAergic
E0060021biological_processroof of mouth development
E0060080biological_processinhibitory postsynaptic potential
E0060119biological_processinner ear receptor cell development
E0060384biological_processinnervation
E0071420biological_processcellular response to histamine
E0071514biological_processgenomic imprinting
E0090102biological_processcochlea development
E0098982cellular_componentGABA-ergic synapse
E0099634cellular_componentpostsynaptic specialization membrane
E0160001biological_processextrasynaptic signaling via GABA
E1902476biological_processchloride transmembrane transport
E1902711cellular_componentGABA-A receptor complex
E1904315molecular_functiontransmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential
E1904862biological_processinhibitory synapse assembly
Functional Information from PROSITE/UniProt
site_idPS00236
Number of Residues15
DetailsNEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMhLedFPmDahaC
ChainResidueDetails
ACYS139-CYS153
CCYS151-CYS165
BCYS136-CYS150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues162
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29950725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues31
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29950725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D6U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62813","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30266951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29950725","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30602789","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D6U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I53","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues170
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35355020","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7QN7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24909990","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues22
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24909990","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24909990","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"35355020","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7QN7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24909990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4COF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"35355020","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7QN7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"30140029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6A96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24909990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30602789","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35355020","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6I53","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7QN7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24909990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30140029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30602789","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35355020","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6A96","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I53","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7QN7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues83
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30602789","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6I53","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29950725","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30602789","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I53","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues80
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

258222

PDB entries from 2026-08-19

PDB statisticsPDBj update infoContact PDBjnumon