Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7XAV

Structure of somatostatin receptor 2 bound with lanreotide.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0004994	molecular_function	somatostatin receptor activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007187	biological_process	G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
A	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A	0007218	biological_process	neuropeptide signaling pathway
A	0008285	biological_process	negative regulation of cell population proliferation
A	0016020	cellular_component	membrane
A	0030165	molecular_function	PDZ domain binding
A	0038170	biological_process	somatostatin signaling pathway
A	0042923	molecular_function	neuropeptide binding
A	0043005	cellular_component	neuron projection
A	0071385	biological_process	cellular response to glucocorticoid stimulus
A	0071392	biological_process	cellular response to estradiol stimulus
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0001664	molecular_function	G protein-coupled receptor binding
B	0003924	molecular_function	GTPase activity
B	0003925	molecular_function	G protein activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005765	cellular_component	lysosomal membrane
B	0005794	cellular_component	Golgi apparatus
B	0005813	cellular_component	centrosome
B	0005829	cellular_component	cytosol
B	0005834	cellular_component	heterotrimeric G-protein complex
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0005938	cellular_component	cell cortex
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
B	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
B	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor signaling pathway
B	0007218	biological_process	neuropeptide signaling pathway
B	0010854	molecular_function	adenylate cyclase regulator activity
B	0010855	molecular_function	adenylate cyclase inhibitor activity
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0019001	molecular_function	guanyl nucleotide binding
B	0019003	molecular_function	GDP binding
B	0030496	cellular_component	midbody
B	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
B	0031749	molecular_function	D2 dopamine receptor binding
B	0031821	molecular_function	G protein-coupled serotonin receptor binding
B	0034451	cellular_component	centriolar satellite
B	0034695	biological_process	response to prostaglandin E
B	0036064	cellular_component	ciliary basal body
B	0043434	biological_process	response to peptide hormone
B	0045542	biological_process	positive regulation of cholesterol biosynthetic process
B	0046676	biological_process	negative regulation of insulin secretion
B	0046872	molecular_function	metal ion binding
B	0051301	biological_process	cell division
B	0060236	biological_process	regulation of mitotic spindle organization
B	0070062	cellular_component	extracellular exosome
B	0070098	biological_process	chemokine-mediated signaling pathway
B	0072678	biological_process	T cell migration
B	1901082	biological_process	positive regulation of relaxation of smooth muscle
B	1904322	biological_process	cellular response to forskolin
B	1904778	biological_process	positive regulation of protein localization to cell cortex
C	0001750	cellular_component	photoreceptor outer 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	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
C	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
C	0008283	biological_process	cell population proliferation
C	0016020	cellular_component	membrane
C	0030159	molecular_function	signaling receptor complex adaptor activity
C	0044877	molecular_function	protein-containing complex binding
C	0045202	cellular_component	synapse
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	0071380	biological_process	cellular response to prostaglandin E stimulus
C	0071870	biological_process	cellular response to catecholamine stimulus
C	0097381	cellular_component	photoreceptor disc membrane
D	0003924	molecular_function	GTPase activity
D	0005515	molecular_function	protein binding
D	0005834	cellular_component	heterotrimeric G-protein complex
D	0005886	cellular_component	plasma membrane
D	0007165	biological_process	signal transduction
D	0007186	biological_process	G protein-coupled receptor signaling pathway
D	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
D	0016020	cellular_component	membrane
D	0031681	molecular_function	G-protein beta-subunit binding
D	0071380	biological_process	cellular response to prostaglandin E stimulus
D	0071870	biological_process	cellular response to catecholamine stimulus

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. TSIfCLTVMSIDRYLaV

Chain	Residue	Details
A	THR128-VAL144

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	55
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	23
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	21
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	14
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Site: {"description":"Important for ligand binding"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	13
Details	Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
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_FI13
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_FI14
Number of Residues	5
Details	Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18434541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22383884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Deamidated glutamine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylcysteine; by pertussis toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	48
Details	Repeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	45
Details	Repeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	40
Details	Repeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	41
Details	Repeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	43
Details	Repeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	41
Details	Repeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	30
Details	Repeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Modified residue: {"description":"Phosphohistidine","evidences":[{"source":"PubMed","id":"12486123","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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