Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QE0

A Galpha-i1 P-loop mutation prevents transition to the activated state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0001664	molecular_function	G protein-coupled receptor binding
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005813	cellular_component	centrosome
A	0005834	cellular_component	heterotrimeric G-protein complex
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005938	cellular_component	cell cortex
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	0016020	cellular_component	membrane
A	0019001	molecular_function	guanyl nucleotide binding
A	0019003	molecular_function	GDP binding
A	0030496	cellular_component	midbody
A	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
A	0031749	molecular_function	D2 dopamine receptor binding
A	0031821	molecular_function	G protein-coupled serotonin receptor binding
A	0043434	biological_process	response to peptide hormone
A	0043949	biological_process	regulation of cAMP-mediated signaling
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division
A	0060236	biological_process	regulation of mitotic spindle organization
A	0070062	cellular_component	extracellular exosome
A	0072678	biological_process	T cell migration
A	1904322	biological_process	cellular response to forskolin
A	1904778	biological_process	positive regulation of protein localization to cell cortex
B	0000287	molecular_function	magnesium ion binding
B	0001664	molecular_function	G protein-coupled receptor binding
B	0003924	molecular_function	GTPase 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	0005813	cellular_component	centrosome
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	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B	0016020	cellular_component	membrane
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	0043434	biological_process	response to peptide hormone
B	0043949	biological_process	regulation of cAMP-mediated signaling
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	0072678	biological_process	T cell migration
B	1904322	biological_process	cellular response to forskolin
B	1904778	biological_process	positive regulation of protein localization to cell cortex
C	0000287	molecular_function	magnesium ion binding
C	0001664	molecular_function	G protein-coupled receptor binding
C	0003924	molecular_function	GTPase activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005765	cellular_component	lysosomal membrane
C	0005813	cellular_component	centrosome
C	0005834	cellular_component	heterotrimeric G-protein complex
C	0005856	cellular_component	cytoskeleton
C	0005886	cellular_component	plasma membrane
C	0005938	cellular_component	cell cortex
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	0016020	cellular_component	membrane
C	0019001	molecular_function	guanyl nucleotide binding
C	0019003	molecular_function	GDP binding
C	0030496	cellular_component	midbody
C	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
C	0031749	molecular_function	D2 dopamine receptor binding
C	0031821	molecular_function	G protein-coupled serotonin receptor binding
C	0043434	biological_process	response to peptide hormone
C	0043949	biological_process	regulation of cAMP-mediated signaling
C	0046872	molecular_function	metal ion binding
C	0051301	biological_process	cell division
C	0060236	biological_process	regulation of mitotic spindle organization
C	0070062	cellular_component	extracellular exosome
C	0072678	biological_process	T cell migration
C	1904322	biological_process	cellular response to forskolin
C	1904778	biological_process	positive regulation of protein localization to cell cortex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 556

Chain	Residue
A	SER47
A	THR181
A	GDP555

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP A 555

Chain	Residue
A	SER47
A	THR48
A	SER151
A	LEU175
A	ARG176
A	THR177
A	ARG178
A	ASN269
A	LYS270
A	ASP272
A	LEU273
A	CYS325
A	ALA326
A	THR327
A	MG556
A	HOH7
A	ARG42
A	GLU43
A	SER44
A	GLY45
A	LYS46

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 556

Chain	Residue
B	SER47
B	GDP355

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP B 355

Chain	Residue
B	GLU43
B	SER44
B	GLY45
B	LYS46
B	SER47
B	THR48
B	SER151
B	LEU175
B	ARG176
B	THR177
B	ARG178
B	ASN269
B	LYS270
B	ASP272
B	LEU273
B	CYS325
B	ALA326
B	THR327
B	MG556

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 552

Chain	Residue
C	SER47
C	VAL179
C	THR181
C	GDP551

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP C 551

Chain	Residue
C	ALA41
C	ARG42
C	GLU43
C	SER44
C	GLY45
C	LYS46
C	SER47
C	THR48
C	SER151
C	LEU175
C	ARG176
C	THR177
C	ARG178
C	ASN269
C	LYS270
C	ASP272
C	LEU273
C	CYS325
C	ALA326
C	THR327
C	MG552

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486, ECO:0007744\|PDB:1KJY, ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:2XNS, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
A	GLU43
A	ASN269
B	GLU43
B	ASN269
C	GLU43
C	ASN269

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:18434541, ECO:0000269\|PubMed:22383884, ECO:0007744\|PDB:3QE0

Chain	Residue	Details
A	SER47
A	THR181
B	SER47
B	THR181
C	SER47
C	THR181

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744\|PDB:1KJY, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:2XNS, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
A	SER151
B	SER151
C	SER151

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744\|PDB:1KJY, ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:2XNS, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
A	LEU175
B	LEU175
C	LEU175

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486

Chain	Residue	Details
A	ASP200
B	ASP200
C	ASP200

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
A	ALA326
B	ALA326
C	ALA326

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
A	ARG178
B	ARG178
C	ARG178

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
A	GLN204
B	GLN204
C	GLN204

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
A	CYS351
B	CYS351
C	CYS351

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