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7F2O

Cryo-EM structure of the type 2 bradykinin receptor in complex with the bradykinin and an Gq protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
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
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
R0004930molecular_functionG protein-coupled receptor activity
R0004947molecular_functionbradykinin receptor activity
R0005506molecular_functioniron ion binding
R0006939biological_processsmooth muscle contraction
R0007186biological_processG protein-coupled receptor signaling pathway
R0009055molecular_functionelectron transfer activity
R0016020cellular_componentmembrane
R0020037molecular_functionheme binding
R0022900biological_processelectron transport chain
R0042310biological_processvasoconstriction
R0042597cellular_componentperiplasmic space
Y0003924molecular_functionGTPase activity
Y0005515molecular_functionprotein binding
Y0005834cellular_componentheterotrimeric G-protein complex
Y0005886cellular_componentplasma membrane
Y0007165biological_processsignal transduction
Y0007186biological_processG protein-coupled receptor signaling pathway
Y0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
Y0016020cellular_componentmembrane
Y0031681molecular_functionG-protein beta-subunit binding
Y0071380biological_processcellular response to prostaglandin E stimulus
Y0071870biological_processcellular response to catecholamine stimulus
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSIwFLMLVSIDRYLaL
ChainResidueDetails
RSER143-LEU159

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
BVAL327-GLY341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by ACE => ECO:0000269|PubMed:4322742, ECO:0000269|PubMed:6055465
ChainResidueDetails
DPRO7

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by kallikrein => ECO:0000303|PubMed:3366244
ChainResidueDetails
DARG9
RASP154-LYS175
RGLN249-ARG267

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 4-hydroxyproline; partial => ECO:0000269|PubMed:3182782, ECO:0000269|PubMed:3366244
ChainResidueDetails
DPRO3

site_idSWS_FT_FI4
Number of Residues52
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RASN119-ARG131
RLYS199-GLU221
RASP293-ASP311

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RVAL132-ILE153

site_idSWS_FT_FI6
Number of Residues22
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RLEU176-MET198

site_idSWS_FT_FI7
Number of Residues26
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RVAL222-MET248

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RALA268-LEU292

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RVAL312-VAL335

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P25023
ChainResidueDetails
RTYR156
RTYR347

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P25023
ChainResidueDetails
RSER366

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P25023
ChainResidueDetails
RTHR369

site_idSWS_FT_FI13
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
RCYS351

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN207

222624

PDB entries from 2024-07-17

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