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9LLZ

Cryo-EM structure of a class C GPCR (Global, without symmetry)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001640molecular_functionadenylate cyclase inhibiting G protein-coupled glutamate receptor activity
A0004930molecular_functionG protein-coupled receptor activity
A0005515molecular_functionprotein binding
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0007196biological_processadenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway
A0007216biological_processG protein-coupled glutamate receptor signaling pathway
A0007268biological_processchemical synaptic transmission
A0007626biological_processlocomotory behavior
A0008066molecular_functionglutamate receptor activity
A0009584biological_processdetection of visible light
A0030425cellular_componentdendrite
A0035841cellular_componentnew growing cell tip
A0042803molecular_functionprotein homodimerization activity
A0045202cellular_componentsynapse
A0050908biological_processdetection of light stimulus involved in visual perception
A0050953biological_processsensory perception of light stimulus
A0051286cellular_componentcell tip
A0051966biological_processregulation of synaptic transmission, glutamatergic
A1905665biological_processpositive regulation of calcium ion import across plasma membrane
B0000139cellular_componentGolgi membrane
B0001640molecular_functionadenylate cyclase inhibiting G protein-coupled glutamate receptor activity
B0004930molecular_functionG protein-coupled receptor activity
B0005515molecular_functionprotein binding
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0007196biological_processadenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway
B0007216biological_processG protein-coupled glutamate receptor signaling pathway
B0007268biological_processchemical synaptic transmission
B0007626biological_processlocomotory behavior
B0008066molecular_functionglutamate receptor activity
B0009584biological_processdetection of visible light
B0030425cellular_componentdendrite
B0035841cellular_componentnew growing cell tip
B0042803molecular_functionprotein homodimerization activity
B0045202cellular_componentsynapse
B0050908biological_processdetection of light stimulus involved in visual perception
B0050953biological_processsensory perception of light stimulus
B0051286cellular_componentcell tip
B0051966biological_processregulation of synaptic transmission, glutamatergic
B1905665biological_processpositive regulation of calcium ion import across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00041
Number of Residues43
DetailsHTH_ARAC_FAMILY_1 Bacterial regulatory proteins, araC family signature. RVvaVVgaSassvsim..VaNVLRLfAIpqis.YastAPElsDsTR
ChainResidueDetails
BARG144-ARG186

site_idPS00979
Number of Residues19
DetailsG_PROTEIN_RECEP_F3_1 G-protein coupled receptors family 3 signature 1. VaNVLrLFaIPQISyASTA
ChainResidueDetails
BVAL160-ALA178

site_idPS00980
Number of Residues23
DetailsG_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCWhCeaCdgyrFqv...DefTCeaC
ChainResidueDetails
BCYS536-CYS558

site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKpIGFTM
ChainResidueDetails
BPHE779-MET789

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
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 Residues102
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues36
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 Residues42
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

255900

PDB entries from 2026-07-01

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