Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4EKD

Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001501	biological_process	skeletal system development
A	0001508	biological_process	action potential
A	0001664	molecular_function	G protein-coupled receptor binding
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005096	molecular_function	GTPase activator activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005794	cellular_component	Golgi apparatus
A	0005834	cellular_component	heterotrimeric G-protein complex
A	0005886	cellular_component	plasma membrane
A	0005901	cellular_component	caveola
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	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
A	0007206	biological_process	phospholipase C-activating G protein-coupled glutamate receptor signaling pathway
A	0007207	biological_process	phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
A	0007208	biological_process	phospholipase C-activating serotonin receptor signaling pathway
A	0007215	biological_process	glutamate receptor signaling pathway
A	0007218	biological_process	neuropeptide signaling pathway
A	0007507	biological_process	heart development
A	0008217	biological_process	regulation of blood pressure
A	0009755	biological_process	hormone-mediated signaling pathway
A	0009791	biological_process	post-embryonic development
A	0010543	biological_process	regulation of platelet activation
A	0016020	cellular_component	membrane
A	0016322	biological_process	neuron remodeling
A	0016787	molecular_function	hydrolase activity
A	0019001	molecular_function	guanyl nucleotide binding
A	0021884	biological_process	forebrain neuron development
A	0030234	molecular_function	enzyme regulator activity
A	0030425	cellular_component	dendrite
A	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
A	0031965	cellular_component	nuclear membrane
A	0032024	biological_process	positive regulation of insulin secretion
A	0034695	biological_process	response to prostaglandin E
A	0042711	biological_process	maternal behavior
A	0042733	biological_process	embryonic digit morphogenesis
A	0043066	biological_process	negative regulation of apoptotic process
A	0043267	biological_process	negative regulation of potassium ion transport
A	0044297	cellular_component	cell body
A	0044877	molecular_function	protein-containing complex binding
A	0045634	biological_process	regulation of melanocyte differentiation
A	0046872	molecular_function	metal ion binding
A	0047391	molecular_function	alkylglycerophosphoethanolamine phosphodiesterase activity
A	0048066	biological_process	developmental pigmentation
A	0050821	biological_process	protein stabilization
A	0060158	biological_process	phospholipase C-activating dopamine receptor signaling pathway
A	0060828	biological_process	regulation of canonical Wnt signaling pathway
A	0071468	biological_process	cellular response to acidic pH
A	0086100	biological_process	endothelin receptor signaling pathway
A	0098793	cellular_component	presynapse
A	0099524	cellular_component	postsynaptic cytosol
A	0140582	biological_process	adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway
A	1904888	biological_process	cranial skeletal system development
A	1990806	biological_process	ligand-gated ion channel signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDP A 401

Chain	Residue
A	GLU49
A	VAL182
A	CYS183
A	ASN274
A	LYS275
A	ASP277
A	LEU278
A	CYS330
A	ALA331
A	THR332
A	ALF402
A	SER50
A	MG407
A	HOH502
A	HOH503
A	GLY51
A	LYS52
A	SER53
A	THR54
A	SER156
A	LEU180
A	ARG181

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ALF A 402

Chain	Residue
A	GLY48
A	GLU49
A	LYS52
A	SER53
A	PRO185
A	THR186
A	GLY208
A	GLN209
A	GDP401
A	MG407
A	HOH501
A	HOH502
A	HOH503

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO A 403

Chain	Residue
A	HIS105
A	HIS109
A	CL404
A	CL405

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 404

Chain	Residue
A	HIS109
A	CO403
A	CL405

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 405

Chain	Residue
A	HIS105
A	HIS109
A	CO403
A	CL404

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO A 406

Chain	Residue
A	ASP319
A	ASP321
B	LYS142

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 407

Chain	Residue
A	SER53
A	THR186
A	GDP401
A	ALF402
A	HOH502
A	HOH503

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MES B 301

Chain	Residue
A	GLU119
A	LYS120
A	LYS133
A	ASP165
B	ASP85
B	TRP113
B	LYS120
B	GLN174
B	TYR178

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	8
Details	Region: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
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_FI5
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_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20966218","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SQ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20966218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SQ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"5-glutamyl histamine","evidences":[{"source":"PubMed","id":"23022564","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	116
Details	Domain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	37
Details	Region: {"description":"Necessary to inhibit protein synthesis","evidences":[{"source":"PubMed","id":"19736320","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)