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6KPF

Cryo-EM structure of a class A GPCR with G protein complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005813cellular_componentcentrosome
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0019001molecular_functionguanyl nucleotide binding
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031749molecular_functionD2 dopamine receptor binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0043434biological_processresponse to peptide hormone
A0043949biological_processregulation of cAMP-mediated signaling
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
C0005515molecular_functionprotein binding
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0016020cellular_componentmembrane
C0031681molecular_functionG-protein beta-subunit binding
C0048144biological_processfibroblast proliferation
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
R0001975biological_processresponse to amphetamine
R0004930molecular_functionG protein-coupled receptor activity
R0004949molecular_functioncannabinoid receptor activity
R0005515molecular_functionprotein binding
R0005737cellular_componentcytoplasm
R0005783cellular_componentendoplasmic reticulum
R0005886cellular_componentplasma membrane
R0006954biological_processinflammatory response
R0006955biological_processimmune response
R0007186biological_processG protein-coupled receptor signaling pathway
R0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0019222biological_processregulation of metabolic process
R0030425cellular_componentdendrite
R0030595biological_processleukocyte chemotaxis
R0031234cellular_componentextrinsic component of cytoplasmic side of plasma membrane
R0032229biological_processnegative regulation of synaptic transmission, GABAergic
R0032496biological_processresponse to lipopolysaccharide
R0033004biological_processnegative regulation of mast cell activation
R0038171biological_processcannabinoid signaling pathway
R0042995cellular_componentcell projection
R0043025cellular_componentneuronal cell body
R0043204cellular_componentperikaryon
R0045759biological_processnegative regulation of action potential
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue E3R R 401
ChainResidue
RTYR25
RPRO184
RILE186
RTRP194
RPHE281
RSER285
RCYS288
RPHE87
RSER90
RPHE91
RPHE94
RVAL113
RTHR114
RPHE117
RPHE183

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVgSLLLTAIDRYLcL
ChainResidueDetails
RALA119-LEU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues69
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RMET1-LYS33
RASN93-ALA104
RTHR173-ASN188
RSER268-LYS279

site_idSWS_FT_FI2
Number of Residues25
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
RTHR34-LEU59
ATHR181

site_idSWS_FT_FI3
Number of Residues119
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
RSER60-LEU71
RASP130-ARG149
RLYS215-THR246
RARG302-CYS360

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
RPHE72-VAL92

site_idSWS_FT_FI5
Number of Residues24
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RVAL105-ILE129

site_idSWS_FT_FI6
Number of Residues22
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RALA150-TRP172

site_idSWS_FT_FI7
Number of Residues25
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RASP189-TRP214

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RLEU247-HIS267

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RALA280-LEU301

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47936
ChainResidueDetails
RSER335
RSER336

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P47936
ChainResidueDetails
RTHR338

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10400664
ChainResidueDetails
RSER352

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN11

219140

PDB entries from 2024-05-01

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