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6W2X

CryoEM Structure of Inactive GABAB Heterodimer

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004965molecular_functionG protein-coupled GABA receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0004888molecular_functiontransmembrane signaling receptor activity
B0004930molecular_functionG protein-coupled receptor activity
B0004965molecular_functionG protein-coupled GABA receptor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B0007194biological_processnegative regulation of adenylate cyclase activity
B0007214biological_processgamma-aminobutyric acid signaling pathway
B0007268biological_processchemical synaptic transmission
B0016020cellular_componentmembrane
B0016917molecular_functionGABA receptor activity
B0038039cellular_componentG protein-coupled receptor heterodimeric complex
B0043005cellular_componentneuron projection
B0045202cellular_componentsynapse
B0045211cellular_componentpostsynaptic membrane
B0046982molecular_functionprotein heterodimerization activity
B0051932biological_processsynaptic transmission, GABAergic
B0150099biological_processneuron-glial cell signaling
B1902710cellular_componentGABA receptor complex
B1902712cellular_componentG protein-coupled GABA receptor complex
Functional Information from PROSITE/UniProt
site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. LNDSKyIGMSV
ChainResidueDetails
BLEU686-VAL696

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 Residues64
DetailsTopological domain: {"description":"Cytoplasmic","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 Residues35
DetailsTopological domain: {"description":"Extracellular","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 Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24305054","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MRM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24305054","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MS4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24305054","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MR7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24305054","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22660477","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22660477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24305054","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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