Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OM2

Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif Of Rgs14

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	0005096	molecular_function	GTPase activator activity
B	0030695	molecular_function	GTPase regulator activity
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	0005096	molecular_function	GTPase activator activity
D	0030695	molecular_function	GTPase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 800

Chain	Residue
A	GDP355
A	HOH4062
B	HOH4158

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 801

Chain	Residue
C	GDP356
C	LYS1046
C	ASP1200
C	GLY1202

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GDP A 355

Chain	Residue
A	SER44
A	GLY45
A	LYS46
A	SER47
A	THR48
A	ASP150
A	SER151
A	ARG176
A	ARG178
A	ASN269
A	LYS270
A	ASP272
A	LEU273
A	CYS325
A	ALA326
A	THR327
A	MG800
A	HOH4032
A	HOH4089
A	HOH4120
B	ARG516
A	ALA41
A	GLU43

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GDP C 356

Chain	Residue
C	MG801
C	ALA1041
C	GLY1042
C	GLU1043
C	SER1044
C	GLY1045
C	LYS1046
C	SER1047
C	THR1048
C	ASP1150
C	SER1151
C	ARG1176
C	ARG1178
C	ASN1269
C	LYS1270
C	ASP1272
C	LEU1273
C	CYS1325
C	ALA1326
C	THR1327
C	HOH4086
C	HOH4087
C	HOH4108
D	ARG1516

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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
C	GLU1043
C	ASN1269

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:18434541, ECO:0000269\|PubMed:22383884, ECO:0007744\|PDB:3QE0

Chain	Residue	Details
C	SER1047
C	THR1181
A	SER47
A	THR181

site_id	SWS_FT_FI3
Number of Residues	2
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
C	SER1151

site_id	SWS_FT_FI4
Number of Residues	2
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
C	LEU1175

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486

Chain	Residue	Details
A	ASP200
C	ASP1200

site_id	SWS_FT_FI6
Number of Residues	2
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
C	ALA1326

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
A	ARG178
C	ARG1178

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
A	GLN204
C	GLN1204

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
A	CYS351
C	CYS1351

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