Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4G5Q

Structure of LGN GL4/Galphai1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0007049	biological_process	cell cycle
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	1904322	biological_process	cellular response to forskolin
A	1904778	biological_process	positive regulation of protein localization to cell cortex
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	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	0007049	biological_process	cell cycle
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	1904322	biological_process	cellular response to forskolin
B	1904778	biological_process	positive regulation of protein localization to cell cortex
C	0000166	molecular_function	nucleotide binding
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	0007049	biological_process	cell cycle
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	1904322	biological_process	cellular response to forskolin
C	1904778	biological_process	positive regulation of protein localization to cell cortex
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0001664	molecular_function	G protein-coupled receptor binding
D	0003924	molecular_function	GTPase activity
D	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0005765	cellular_component	lysosomal membrane
D	0005813	cellular_component	centrosome
D	0005834	cellular_component	heterotrimeric G-protein complex
D	0005856	cellular_component	cytoskeleton
D	0005886	cellular_component	plasma membrane
D	0005938	cellular_component	cell cortex
D	0007049	biological_process	cell cycle
D	0007165	biological_process	signal transduction
D	0007186	biological_process	G protein-coupled receptor signaling pathway
D	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
D	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
D	0016020	cellular_component	membrane
D	0019001	molecular_function	guanyl nucleotide binding
D	0019003	molecular_function	GDP binding
D	0030496	cellular_component	midbody
D	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
D	0031749	molecular_function	D2 dopamine receptor binding
D	0031821	molecular_function	G protein-coupled serotonin receptor binding
D	0043434	biological_process	response to peptide hormone
D	0043949	biological_process	regulation of cAMP-mediated signaling
D	0046872	molecular_function	metal ion binding
D	0051301	biological_process	cell division
D	0060236	biological_process	regulation of mitotic spindle organization
D	0070062	cellular_component	extracellular exosome
D	1904322	biological_process	cellular response to forskolin
D	1904778	biological_process	positive regulation of protein localization to cell cortex
E	0030695	molecular_function	GTPase regulator activity
F	0030695	molecular_function	GTPase regulator activity
G	0030695	molecular_function	GTPase regulator activity
H	0030695	molecular_function	GTPase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GDP A 401

Chain	Residue
A	GLY42
A	ARG176
A	ARG178
A	ASN269
A	LYS270
A	ASP272
A	LEU273
A	CYS325
A	ALA326
A	THR327
E	ARG635
A	GLU43
E	ARG640
A	SER44
A	GLY45
A	LYS46
A	SER47
A	THR48
A	ASP150
A	SER151

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	LYS35
A	LYS197
A	HIS213

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	THR170
A	GLN171

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	SER263
A	TYR320
A	ASN346

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 405

Chain	Residue
A	SER293
A	ASN294

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GDP B 401

Chain	Residue
B	GLY42
B	GLU43
B	SER44
B	GLY45
B	LYS46
B	SER47
B	THR48
B	ASP150
B	SER151
B	ARG176
B	ARG178
B	ASN269
B	LYS270
B	ASP272
B	LEU273
B	CYS325
B	ALA326
B	THR327
F	ARG635
F	ARG640

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT B 402

Chain	Residue
A	LYS271
A	HIS322
A	PHE323
A	ASN331
A	PHE334
B	GLU275
B	LYS279
B	THR295
B	TYR296
B	GLU297

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT B 403

Chain	Residue
A	GLU275
A	THR295
A	TYR296
A	GLU297
A	HOH502
B	LYS271
B	HIS322
B	PHE323
B	ASN331
B	VAL335

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 404

Chain	Residue
B	LYS35
B	LYS197
B	PHE199
B	HIS213

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 405

Chain	Residue
B	THR170
B	GLN171

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 406

Chain	Residue
B	SER263
B	TYR320
B	ASN346

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 407

Chain	Residue
B	LYS128
B	LYS132

site_id	BC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP C 401

Chain	Residue
C	THR327
G	ARG635
G	ARG640
C	ALA41
C	GLY42
C	GLU43
C	SER44
C	GLY45
C	LYS46
C	SER47
C	THR48
C	ASP150
C	SER151
C	ARG176
C	ARG178
C	ASN269
C	LYS270
C	ASP272
C	LEU273
C	CYS325
C	ALA326

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CIT C 402

Chain	Residue
C	GLU275
C	LYS279
C	THR295
C	TYR296
C	GLU297
D	LYS271
D	HIS322
D	PHE323
D	ASN331
D	PHE334
D	VAL335

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 403

Chain	Residue
C	GLU33
C	LYS35
C	LYS197
C	PHE199
C	HIS213

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 404

Chain	Residue
C	THR170
C	GLN171

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 405

Chain	Residue
C	PHE191
C	LYS192

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 406

Chain	Residue
C	SER293
C	ASN294

site_id	CC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GDP D 401

Chain	Residue
D	GLU43
D	SER44
D	GLY45
D	LYS46
D	SER47
D	THR48
D	ASP150
D	SER151
D	ARG176
D	ARG178
D	ASN269
D	LYS270
D	ASP272
D	LEU273
D	CYS325
D	ALA326
D	THR327
D	HOH506
H	ARG635
H	ARG640

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT D 402

Chain	Residue
C	LYS271
C	HIS322
C	PHE323
C	ASN331
C	VAL335
D	GLU275
D	THR295
D	TYR296
D	GLU297

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 403

Chain	Residue
D	ASP158
D	ARG161
D	ASN166

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 404

Chain	Residue
D	LYS35
D	LYS197
D	PHE199
D	HIS213

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 D 405

Chain	Residue
D	LYS128

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 406

Chain	Residue
D	PHE191
D	LYS192

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 407

Chain	Residue
D	ASN255
D	LYS312

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:22952234, ECO:0007744\|PDB:4G5O, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
E	ARG635
E	ARG640
F	ARG635
F	ARG640
G	ARG635
G	ARG640
H	ARG635
H	ARG640

site_id	SWS_FT_FI2
Number of Residues	8
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
D	SER47
D	THR181

site_id	SWS_FT_FI3
Number of Residues	4
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
D	SER151

site_id	SWS_FT_FI4
Number of Residues	4
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
D	LEU175

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486

Chain	Residue	Details
A	ASP200
B	ASP200
C	ASP200
D	ASP200

site_id	SWS_FT_FI6
Number of Residues	4
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
D	ALA326

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
A	ARG178
B	ARG178
C	ARG178
D	ARG178

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
A	GLN204
B	GLN204
C	GLN204
D	GLN204

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
A	CYS351
B	CYS351
C	CYS351
D	CYS351

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