Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7JJO

Structural Basis of the Activation of Heterotrimeric Gs-protein by Isoproterenol-bound Beta1-Adrenergic Receptor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003924	molecular_function	GTPase activity
A	0005159	molecular_function	insulin-like growth factor receptor binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005834	cellular_component	heterotrimeric G-protein complex
A	0005886	cellular_component	plasma membrane
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
A	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
A	0007606	biological_process	sensory perception of chemical stimulus
A	0010856	molecular_function	adenylate cyclase activator activity
A	0016787	molecular_function	hydrolase activity
A	0019001	molecular_function	guanyl nucleotide binding
A	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
A	0031698	molecular_function	beta-2 adrenergic receptor binding
A	0031748	molecular_function	D1 dopamine receptor binding
A	0031852	molecular_function	mu-type opioid receptor binding
A	0035255	molecular_function	ionotropic glutamate receptor binding
A	0046872	molecular_function	metal ion binding
A	0051430	molecular_function	corticotropin-releasing hormone receptor 1 binding
A	0071880	biological_process	adenylate cyclase-activating adrenergic receptor signaling pathway
B	0001750	cellular_component	photoreceptor outer segment
B	0003924	molecular_function	GTPase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005834	cellular_component	heterotrimeric G-protein complex
B	0005886	cellular_component	plasma membrane
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
B	0016020	cellular_component	membrane
B	0030159	molecular_function	signaling receptor complex adaptor activity
B	0044877	molecular_function	protein-containing complex binding
B	0045202	cellular_component	synapse
B	0051020	molecular_function	GTPase binding
B	0071380	biological_process	cellular response to prostaglandin E stimulus
B	0071870	biological_process	cellular response to catecholamine stimulus
B	0097381	cellular_component	photoreceptor disc membrane
G	0003924	molecular_function	GTPase activity
G	0005515	molecular_function	protein binding
G	0005834	cellular_component	heterotrimeric G-protein complex
G	0005886	cellular_component	plasma membrane
G	0007165	biological_process	signal transduction
G	0007186	biological_process	G protein-coupled receptor signaling pathway
G	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
G	0016020	cellular_component	membrane
G	0031681	molecular_function	G-protein beta-subunit binding
G	0071380	biological_process	cellular response to prostaglandin E stimulus
G	0071870	biological_process	cellular response to catecholamine stimulus
R	0003796	molecular_function	lysozyme activity
R	0004930	molecular_function	G protein-coupled receptor activity
R	0007186	biological_process	G protein-coupled receptor signaling pathway
R	0009253	biological_process	peptidoglycan catabolic process
R	0016020	cellular_component	membrane
R	0016998	biological_process	cell wall macromolecule catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAIDRYLaI

Chain	Residue	Details
R	ALA127-ILE143

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

Chain	Residue	Details
B	LEU70-SER84
B	ILE157-ILE171
B	LEU285-ALA299

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Repeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	45
Details	Repeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Repeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	41
Details	Repeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	43
Details	Repeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	41
Details	Repeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	30
Details	Repeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphohistidine","evidences":[{"source":"PubMed","id":"12486123","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	9
Details	Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	7
Details	Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	25
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	26
Details	Transmembrane: {"description":"Helical; Name=2"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	40
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=3"}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=4"}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	25
Details	Transmembrane: {"description":"Helical; Name=5"}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	29
Details	Transmembrane: {"description":"Helical; Name=6"}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=7"}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VT4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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