Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3C7K

Molecular architecture of Galphao and the structural basis for RGS16-mediated deactivation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005102	molecular_function	signaling receptor binding
A	0005515	molecular_function	protein 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	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
A	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor signaling pathway
A	0007212	biological_process	G protein-coupled dopamine receptor signaling pathway
A	0007626	biological_process	locomotory behavior
A	0008016	biological_process	regulation of heart contraction
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019001	molecular_function	guanyl nucleotide binding
A	0030425	cellular_component	dendrite
A	0030672	cellular_component	synaptic vesicle membrane
A	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
A	0031821	molecular_function	G protein-coupled serotonin receptor binding
A	0031852	molecular_function	mu-type opioid receptor binding
A	0032794	molecular_function	GTPase activating protein binding
A	0042734	cellular_component	presynaptic membrane
A	0043209	cellular_component	myelin sheath
A	0043547	biological_process	positive regulation of GTPase activity
A	0044297	cellular_component	cell body
A	0045211	cellular_component	postsynaptic membrane
A	0046676	biological_process	negative regulation of insulin secretion
A	0046872	molecular_function	metal ion binding
A	0051430	molecular_function	corticotropin-releasing hormone receptor 1 binding
A	0051926	biological_process	negative regulation of calcium ion transport
A	0071867	biological_process	response to monoamine
A	0098688	cellular_component	parallel fiber to Purkinje cell synapse
A	0098978	cellular_component	glutamatergic synapse
A	0098982	cellular_component	GABA-ergic synapse
A	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
A	1904014	biological_process	response to serotonin
C	0000166	molecular_function	nucleotide binding
C	0003924	molecular_function	GTPase activity
C	0003925	molecular_function	G protein activity
C	0005102	molecular_function	signaling receptor binding
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP 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	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
C	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
C	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor signaling pathway
C	0007212	biological_process	G protein-coupled dopamine receptor signaling pathway
C	0007626	biological_process	locomotory behavior
C	0008016	biological_process	regulation of heart contraction
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0019001	molecular_function	guanyl nucleotide binding
C	0030425	cellular_component	dendrite
C	0030672	cellular_component	synaptic vesicle membrane
C	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
C	0031821	molecular_function	G protein-coupled serotonin receptor binding
C	0031852	molecular_function	mu-type opioid receptor binding
C	0032794	molecular_function	GTPase activating protein binding
C	0042734	cellular_component	presynaptic membrane
C	0043209	cellular_component	myelin sheath
C	0043547	biological_process	positive regulation of GTPase activity
C	0044297	cellular_component	cell body
C	0045211	cellular_component	postsynaptic membrane
C	0046676	biological_process	negative regulation of insulin secretion
C	0046872	molecular_function	metal ion binding
C	0051430	molecular_function	corticotropin-releasing hormone receptor 1 binding
C	0051926	biological_process	negative regulation of calcium ion transport
C	0071867	biological_process	response to monoamine
C	0098688	cellular_component	parallel fiber to Purkinje cell synapse
C	0098978	cellular_component	glutamatergic synapse
C	0098982	cellular_component	GABA-ergic synapse
C	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
C	1904014	biological_process	response to serotonin

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 362

Chain	Residue
A	SER47
A	THR182

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ALF A 365

Chain	Residue
A	GLY204
A	GLN205
A	ALA41
A	GLY42
A	GLU43
A	LYS46
A	ARG179
A	LYS181
A	THR182

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 362

Chain	Residue
C	SER47
C	THR182

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ALF C 365

Chain	Residue
C	GLY42
C	GLU43
C	LYS46
C	ARG179
C	LYS181
C	THR182
C	GLY204
C	GLN205

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP A 361

Chain	Residue
A	GLU43
A	SER44
A	GLY45
A	LYS46
A	SER47
A	THR48
A	ASP151
A	SER152
A	LEU176
A	ARG177
A	THR178
A	ARG179
A	ASN270
A	LYS271
A	ASP273
A	LEU274
A	CYS325
A	ALA326
A	THR327

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GDP C 361

Chain	Residue
C	GLU43
C	SER44
C	GLY45
C	LYS46
C	SER47
C	THR48
C	ASP151
C	SER152
C	LEU176
C	ARG177
C	THR178
C	ARG179
C	ASN270
C	LYS271
C	ASP273
C	LEU274
C	CYS325
C	ALA326

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	26
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	16
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	14
Details	Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	10
Details	Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18434540","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3C7K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18434540","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C7K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"5-glutamyl histamine","evidences":[{"source":"PubMed","id":"23022564","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"UniProtKB","id":"O15492","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O15492","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	ARG179
A	THR182
A	GLU43
A	GLN205

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
C	ARG179
C	THR182
C	GLU43
C	GLN205

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	GLN205

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
C	GLN205

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