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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
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
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 Residues490
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BTRP42-SER483
BVAL544-THR551
BASP619-THR654
BTHR713-GLN720

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
BILE484-ILE504
AHIS572-LEU593
AGLU673-ALA687
APRO738-LYS844

site_idSWS_FT_FI3
Number of Residues255
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BLYS505-LEU522
BALA573-LEU597
BTRP676-TYR691
BPRO742-LEU941

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
BILE523-PHE543
AASP615-THR651
ALEU709-ALA716

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
BLEU552-PHE572

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
BLEU598-VAL618

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
BILE655-ALA675

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
BILE692-LEU712

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
BPHE721-VAL741

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80T41
ChainResidueDetails
BSER776
BSER779
BSER884
BSER893
BSER913
BSER916
BSER920
BSER924

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q80T41
ChainResidueDetails
BTHR819

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22660477
ChainResidueDetails
BASN90
BASN389
BASN453

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN298
ATHR813

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054
ChainResidueDetails
BASN404
AASN292
AASN385
AASN397

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24305054
ChainResidueDetails
AASN323
AASN365

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PDB entries from 2024-07-17

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