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9II3

Cryo-EM Structure of the 2:1 Complex of mGlu3 and beta-arrestin1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000785cellular_componentchromatin
A0001664molecular_functionG protein-coupled receptor binding
A0001934biological_processpositive regulation of protein phosphorylation
A0002031biological_processG protein-coupled receptor internalization
A0002092biological_processpositive regulation of receptor internalization
A0003713molecular_functiontranscription coactivator activity
A0004402molecular_functionhistone acetyltransferase activity
A0004857molecular_functionenzyme inhibitor activity
A0005096molecular_functionGTPase activator activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005905cellular_componentclathrin-coated pit
A0006357biological_processregulation of transcription by RNA polymerase II
A0006511biological_processubiquitin-dependent protein catabolic process
A0009968biological_processnegative regulation of signal transduction
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016604cellular_componentnuclear body
A0030659cellular_componentcytoplasmic vesicle membrane
A0030666cellular_componentendocytic vesicle membrane
A0031143cellular_componentpseudopodium
A0031397biological_processnegative regulation of protein ubiquitination
A0031410cellular_componentcytoplasmic vesicle
A0031625molecular_functionubiquitin protein ligase binding
A0031701molecular_functionangiotensin receptor binding
A0032088biological_processnegative regulation of NF-kappaB transcription factor activity
A0032715biological_processnegative regulation of interleukin-6 production
A0032717biological_processnegative regulation of interleukin-8 production
A0035025biological_processpositive regulation of Rho protein signal transduction
A0042995cellular_componentcell projection
A0043149biological_processstress fiber assembly
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045746biological_processnegative regulation of Notch signaling pathway
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0060090molecular_functionmolecular adaptor activity
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A1990763molecular_functionarrestin family protein binding
Functional Information from PROSITE/UniProt
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
APHE61-LEU79

site_idPS00979
Number of Residues19
DetailsG_PROTEIN_RECEP_F3_1 G-protein coupled receptors family 3 signature 1. VaNLLrLFqIPQISyASTS
ChainResidueDetails
RVAL157-SER175

site_idPS00980
Number of Residues23
DetailsG_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCWiCipCepyeYla...DefTCmdC
ChainResidueDetails
RCYS527-CYS549

site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKfIGFTM
ChainResidueDetails
RPHE765-MET775

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS250
AMET255
ALYS324
ALYS326
BLEU23-TRP576
BLYS635-ARG645
BGLU710-ASP734
BSER793-THR802

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8BWG8
ChainResidueDetails
ATYR47
BALA577-ILE599

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by GRK5 => ECO:0000269|PubMed:19661922, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER412
RCYS665-GLN688
RLYS757-LYS769
RGLN829-LEU879
BLYS600-GLU613
BCYS665-GLN688
BLYS757-LYS769
BGLN829-LEU879

site_idSWS_FT_FI4
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
RLEU614-ALA634
BLEU614-ALA634

site_idSWS_FT_FI5
Number of Residues36
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RLEU646-ASN664
BLEU646-ASN664

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RVAL689-LEU709
BVAL689-LEU709

site_idSWS_FT_FI7
Number of Residues42
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RSER735-PHE756
BSER735-PHE756

site_idSWS_FT_FI8
Number of Residues44
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RPHE770-THR792
BPHE770-THR792

site_idSWS_FT_FI9
Number of Residues50
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RMET803-PHE828
BMET803-PHE828

site_idSWS_FT_FI10
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
RSER151
BLYS389
RALA172
RTYR222
RASP301
RLYS389
BSER151
BALA172
BTYR222
BASP301

site_idSWS_FT_FI11
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN209
RASN292
RASN414
RASN439
BASN209
BASN292
BASN414
BASN439

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PDB entries from 2025-04-30

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