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	0003925	molecular_function	G protein activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005834	cellular_component	heterotrimeric G-protein complex
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	0007189	biological_process	adenylate cyclase-activating 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	0007218	biological_process	neuropeptide signaling pathway
A	0010855	molecular_function	adenylate cyclase inhibitor activity
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
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	0034695	biological_process	response to prostaglandin E
A	0036064	cellular_component	ciliary basal body
A	0043303	biological_process	mast cell degranulation
A	0043434	biological_process	response to peptide hormone
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
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	0070098	biological_process	chemokine-mediated signaling pathway
A	0072678	biological_process	T cell migration
A	1901082	biological_process	positive regulation of relaxation of smooth muscle
A	1903998	biological_process	regulation of eating behavior
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	0003925	molecular_function	G protein activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005765	cellular_component	lysosomal membrane
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0005834	cellular_component	heterotrimeric G-protein complex
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	0007189	biological_process	adenylate cyclase-activating 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	0007218	biological_process	neuropeptide signaling pathway
C	0010855	molecular_function	adenylate cyclase inhibitor activity
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
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	0034695	biological_process	response to prostaglandin E
C	0036064	cellular_component	ciliary basal body
C	0043303	biological_process	mast cell degranulation
C	0043434	biological_process	response to peptide hormone
C	0045542	biological_process	positive regulation of cholesterol biosynthetic process
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	0070098	biological_process	chemokine-mediated signaling pathway
C	0072678	biological_process	T cell migration
C	1901082	biological_process	positive regulation of relaxation of smooth muscle
C	1903998	biological_process	regulation of eating behavior
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	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	18
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	14
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	10
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	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18434541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22383884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylarginine; by cholera toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Deamidated glutamine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	46
Details	Domain: {"description":"GoLoco","evidences":[{"source":"PROSITE-ProRule","id":"PRU00097","evidenceCode":"ECO:0000255"}]}

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	THR181
A	GLN204
A	GLU43
A	ARG178

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

Chain	Residue	Details
C	GLU1043
C	GLN1204
C	ARG1178
C	THR1181

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

Chain	Residue	Details
A	GLN204

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

Chain	Residue	Details
C	GLN1204

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