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7DFL

Cryo-EM structure of histamine H1 receptor Gq complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
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
G0005834cellular_componentheterotrimeric G-protein complex
G0007186biological_processG protein-coupled receptor signaling pathway
G0031681molecular_functionG-protein beta-subunit binding
R0004930molecular_functionG protein-coupled receptor activity
R0004969molecular_functionhistamine receptor activity
R0005829cellular_componentcytosol
R0005886cellular_componentplasma membrane
R0006954biological_processinflammatory response
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0007208biological_processphospholipase C-activating serotonin receptor signaling pathway
R0007268biological_processchemical synaptic transmission
R0007613biological_processmemory
R0008542biological_processvisual learning
R0016020cellular_componentmembrane
R0030425cellular_componentdendrite
R0043114biological_processregulation of vascular permeability
R0045202cellular_componentsynapse
R0045907biological_processpositive regulation of vasoconstriction
R0048167biological_processregulation of synaptic plasticity
R0071420biological_processcellular response to histamine
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfSVFILCIDRYRsV
ChainResidueDetails
RALA113-VAL129

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ACYS3
RMET90-ARG97
RTRP165-THR188
RCYS441-ASN446

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P21279
ChainResidueDetails
ASER50
ATHR186
AASN274
ALYS275
AASP277
AALA331
AGLY51
ALYS52
ASER53
ATHR54
ASER156
ALEU180
AARG181
AARG183

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AGLN209
RASP124-ALA144
RLYS212-GLN416
RLEU470-SER487

site_idSWS_FT_FI4
Number of Residues24
DetailsTRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RTYR65-LEU89

site_idSWS_FT_FI5
Number of Residues25
DetailsTRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RPRO98-ILE123

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=4 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RSER145-GLY164

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RTRP189-ALA211

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RLEU417-PHE440

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RGLU447-PRO469

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:33828102
ChainResidueDetails
RASP107
RASN198

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RTHR112
RTYR431

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:15328002
ChainResidueDetails
RTHR140
RTHR142

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER230

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
RTHR279

site_idSWS_FT_FI15
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P70174
ChainResidueDetails
RSER344
RSER347
RSER380

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15328002
ChainResidueDetails
RSER396
RSER398

site_idSWS_FT_FI17
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN5
RASN18

237735

PDB entries from 2025-06-18

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