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7SHF

Cryo-EM structure of GPR158 coupled to the RGS7-Gbeta5 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0004930molecular_functionG protein-coupled receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
C0001965molecular_functionG-protein alpha-subunit binding
C0001975biological_processresponse to amphetamine
C0003924molecular_functionGTPase activity
C0005096molecular_functionGTPase activator activity
C0005635cellular_componentnuclear envelope
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0008277biological_processregulation of G protein-coupled receptor signaling pathway
C0009968biological_processnegative regulation of signal transduction
C0031681molecular_functionG-protein beta-subunit binding
C0032991cellular_componentprotein-containing complex
C0035556biological_processintracellular signal transduction
C0043005cellular_componentneuron projection
C0043547biological_processpositive regulation of GTPase activity
C0045471biological_processresponse to ethanol
C0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
C1901381biological_processpositive regulation of potassium ion transmembrane transport
D0007165biological_processsignal transduction
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. IVSSsqDgKVIVWDS
ChainResidueDetails
DILE78-SER92
DILE168-VAL182
DLEU298-VAL312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49803
ChainResidueDetails
CSER229
BVAL548-ASP576
BLEU634-TRP642
AALA24-ARG417
AVAL548-ASP576
ALEU634-TRP642

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O54829
ChainResidueDetails
CSER241
ALEU418-TYR439

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54829
ChainResidueDetails
CTHR243
BLYS502-ARG525
BTYR598-ARG611
AHIS440-GLY451
ALYS502-ARG525
ATYR598-ARG611

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10862767
ChainResidueDetails
CSER434
ALEU452-PHE474

site_idSWS_FT_FI5
Number of Residues6
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0000305, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
BGLU475-THR478
AGLU475-THR478

site_idSWS_FT_FI6
Number of Residues44
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
BPHE479-LEU501
APHE479-LEU501

site_idSWS_FT_FI7
Number of Residues42
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
BVAL526-SER547
AVAL526-SER547

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
BARG577-CYS597
AARG577-CYS597

site_idSWS_FT_FI9
Number of Residues42
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
BTYR612-VAL633
ATYR612-VAL633

site_idSWS_FT_FI10
Number of Residues42
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF
ChainResidueDetails
BMET643-ILE664
AMET643-ILE664

site_idSWS_FT_FI11
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:36996198
ChainResidueDetails
BSER172
BARG173
BGLU271
BASP307
ASER172
AARG173
AGLU271
AASP307

site_idSWS_FT_FI12
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C419
ChainResidueDetails
BSER694
BSER705
BSER708
ASER694
ASER705
ASER708

site_idSWS_FT_FI13
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN98
AASN333
BASN143
BASN215
BASN274
BASN333
AASN98
AASN143
AASN215
AASN274

site_idSWS_FT_FI14
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18655026
ChainResidueDetails
BLYS774
ALYS774

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PDB entries from 2024-07-24

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