Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7EIB

Cryo-EM structure of the type 1 bradykinin receptor in complex with the des-Arg10-kallidin and an Gq protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002687	biological_process	positive regulation of leukocyte migration
A	0004930	molecular_function	G protein-coupled receptor activity
A	0004947	molecular_function	bradykinin receptor activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005886	cellular_component	plasma membrane
A	0006954	biological_process	inflammatory response
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007204	biological_process	positive regulation of cytosolic calcium ion concentration
A	0009055	molecular_function	electron transfer activity
A	0009612	biological_process	response to mechanical stimulus
A	0016020	cellular_component	membrane
A	0016477	biological_process	cell migration
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0030308	biological_process	negative regulation of cell growth
A	0032496	biological_process	response to lipopolysaccharide
A	0042277	molecular_function	peptide binding
A	0042597	cellular_component	periplasmic space
A	0045776	biological_process	negative regulation of blood pressure
A	0051281	biological_process	positive regulation of release of sequestered calcium ion into cytosol
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0019001	molecular_function	guanyl nucleotide binding
B	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
C	0001750	cellular_component	photoreceptor outer segment
C	0001917	cellular_component	photoreceptor inner segment
C	0003924	molecular_function	GTPase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005834	cellular_component	heterotrimeric G-protein complex
C	0005886	cellular_component	plasma membrane
C	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
C	0007204	biological_process	positive regulation of cytosolic calcium ion concentration
C	0008283	biological_process	cell population proliferation
C	0010659	biological_process	cardiac muscle cell apoptotic process
C	0030159	molecular_function	signaling receptor complex adaptor activity
C	0030425	cellular_component	dendrite
C	0030507	molecular_function	spectrin binding
C	0042622	cellular_component	photoreceptor outer segment membrane
C	0044297	cellular_component	cell body
C	0044877	molecular_function	protein-containing complex binding
C	0045202	cellular_component	synapse
C	0047391	molecular_function	alkylglycerophosphoethanolamine phosphodiesterase activity
C	0050909	biological_process	sensory perception of taste
C	0051020	molecular_function	GTPase binding
C	0060041	biological_process	retina development in camera-type eye
C	0071456	biological_process	cellular response to hypoxia
E	0003924	molecular_function	GTPase activity
E	0005515	molecular_function	protein binding
E	0005834	cellular_component	heterotrimeric G-protein complex
E	0005886	cellular_component	plasma membrane
E	0007165	biological_process	signal transduction
E	0007186	biological_process	G protein-coupled receptor signaling pathway
E	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
E	0016020	cellular_component	membrane
E	0031681	molecular_function	G-protein beta-subunit binding
E	0071380	biological_process	cellular response to prostaglandin E stimulus
E	0071870	biological_process	cellular response to catecholamine stimulus

Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS

Chain	Residue	Details
C	LEU70-SER84
C	ILE157-ILE171
C	LEU285-ALA299
C	VAL327-GLY341

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	29
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	50
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	26
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	48
Details	Repeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	45
Details	Repeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	40
Details	Repeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	41
Details	Repeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	43
Details	Repeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	41
Details	Repeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	30
Details	Repeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)