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8JCZ

Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and LY2389575 (dimerization mode III)

Functional Information from GO Data
ChainGOidnamespacecontents
20000413biological_processprotein peptidyl-prolyl isomerization
20001641molecular_functiongroup II metabotropic glutamate receptor activity
20003007biological_processheart morphogenesis
20003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
20004930molecular_functionG protein-coupled receptor activity
20005160molecular_functiontransforming growth factor beta receptor binding
20005246molecular_functioncalcium channel regulator activity
20005515molecular_functionprotein binding
20005527molecular_functionmacrolide binding
20005528molecular_functionFK506 binding
20005737cellular_componentcytoplasm
20005829cellular_componentcytosol
20005886cellular_componentplasma membrane
20006457biological_processprotein folding
20006458biological_process'de novo' protein folding
20007186biological_processG protein-coupled receptor signaling pathway
20007194biological_processnegative regulation of adenylate cyclase activity
20007196biological_processadenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway
20007215biological_processglutamate receptor signaling pathway
20007216biological_processG protein-coupled glutamate receptor signaling pathway
20007268biological_processchemical synaptic transmission
20008066molecular_functionglutamate receptor activity
20010467biological_processgene expression
20014047biological_processglutamate secretion
20014048biological_processregulation of glutamate secretion
20014059biological_processregulation of dopamine secretion
20014802cellular_componentterminal cisterna
20014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
20016020cellular_componentmembrane
20016247molecular_functionchannel regulator activity
20016529cellular_componentsarcoplasmic reticulum
20022417biological_processprotein maturation by protein folding
20030018cellular_componentZ disc
20030424cellular_componentaxon
20030425cellular_componentdendrite
20030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
20030547molecular_functionsignaling receptor inhibitor activity
20032092biological_processpositive regulation of protein binding
20032880biological_processregulation of protein localization
20032926biological_processnegative regulation of activin receptor signaling pathway
20033017cellular_componentsarcoplasmic reticulum membrane
20033554biological_processcellular response to stress
20034713molecular_functiontype I transforming growth factor beta receptor binding
20035095biological_processbehavioral response to nicotine
20042026biological_processprotein refolding
20042110biological_processT cell activation
20042220biological_processresponse to cocaine
20042734cellular_componentpresynaptic membrane
20042995cellular_componentcell projection
20043005cellular_componentneuron projection
20043123biological_processpositive regulation of canonical NF-kappaB signal transduction
20044325molecular_functiontransmembrane transporter binding
20045202cellular_componentsynapse
20045211cellular_componentpostsynaptic membrane
20050776biological_processregulation of immune response
20051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
20051966biological_processregulation of synaptic transmission, glutamatergic
20055010biological_processventricular cardiac muscle tissue morphogenesis
20060292biological_processlong-term synaptic depression
20060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
20060347biological_processheart trabecula formation
20070411molecular_functionI-SMAD binding
20070588biological_processcalcium ion transmembrane transport
20070697molecular_functionactivin receptor binding
20090461biological_processintracellular glutamate homeostasis
20097110molecular_functionscaffold protein binding
20097435biological_processsupramolecular fiber organization
20097449cellular_componentastrocyte projection
20098562cellular_componentcytoplasmic side of membrane
20098978cellular_componentglutamatergic synapse
20099171biological_processpresynaptic modulation of chemical synaptic transmission
21902991biological_processregulation of amyloid precursor protein catabolic process
21990000biological_processamyloid fibril formation
21990425cellular_componentryanodine receptor complex
22001023biological_processregulation of response to drug
30001641molecular_functiongroup II metabotropic glutamate receptor activity
30004930molecular_functionG protein-coupled receptor activity
30005246molecular_functioncalcium channel regulator activity
30005886cellular_componentplasma membrane
30007186biological_processG protein-coupled receptor signaling pathway
30007194biological_processnegative regulation of adenylate cyclase activity
30007196biological_processadenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway
30007216biological_processG protein-coupled glutamate receptor signaling pathway
30007268biological_processchemical synaptic transmission
30008066molecular_functionglutamate receptor activity
30010467biological_processgene expression
30014069cellular_componentpostsynaptic density
30016020cellular_componentmembrane
30030424cellular_componentaxon
30033554biological_processcellular response to stress
30042734cellular_componentpresynaptic membrane
30043005cellular_componentneuron projection
30043197cellular_componentdendritic spine
30044877molecular_functionprotein-containing complex binding
30045211cellular_componentpostsynaptic membrane
30051966biological_processregulation of synaptic transmission, glutamatergic
30097110molecular_functionscaffold protein binding
30097449cellular_componentastrocyte projection
30098978cellular_componentglutamatergic synapse
30099170biological_processpostsynaptic modulation of chemical synaptic transmission
Functional Information from PROSITE/UniProt
site_idPS00979
Number of Residues19
DetailsG_PROTEIN_RECEP_F3_1 G-protein coupled receptors family 3 signature 1. VaNLLrLFqIPQISyASTS
ChainResidueDetails
3VAL157-SER175
2VAL151-SER169

site_idPS00980
Number of Residues23
DetailsG_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCWiCipCepyeYla...DefTCmdC
ChainResidueDetails
3CYS527-CYS549
2CYS518-CYS540

site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKfIGFTM
ChainResidueDetails
3PHE765-MET775
2PHE756-MET766

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues596
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
3LEU23-TRP576
3LYS635-ARG645
3GLU710-ASP734
3SER793-THR802

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
3ALA577-ILE599

site_idSWS_FT_FI3
Number of Residues98
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
3LYS600-GLU613
3CYS665-GLN688
3LYS757-LYS769
3GLN829-LEU879

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
3LEU614-ALA634

site_idSWS_FT_FI5
Number of Residues18
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
3LEU646-ASN664

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
3VAL689-LEU709

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
3SER735-PHE756

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
3PHE770-THR792

site_idSWS_FT_FI9
Number of Residues25
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
3MET803-PHE828

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
3SER151
3ALA172
3TYR222
3ASP301
3LYS389

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
3ASN209
3ASN292
3ASN414
3ASN439
2ASN547

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26883
ChainResidueDetails
2LYS932

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 362
ChainResidueDetails
2TYR906electrostatic destabiliser, steric role
2PHE916electrostatic destabiliser, polar/non-polar interaction, steric role
2ASP917electrostatic stabiliser, steric role
2ILE936electrostatic stabiliser, steric role
2TYR962electrostatic stabiliser, steric role
2PHE979electrostatic destabiliser, polar/non-polar interaction, steric role

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PDB entries from 2024-10-30

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