Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZJZ

Structure of the K349P mutant of Gi alpha 1 subunit bound to GDP

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	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	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor 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	0032794	molecular_function	GTPase activating protein binding
A	0032991	cellular_component	protein-containing complex
A	0034695	biological_process	response to prostaglandin E
A	0043303	biological_process	mast cell degranulation
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050805	biological_process	negative regulation of synaptic transmission
A	0051301	biological_process	cell division
A	0060236	biological_process	regulation of mitotic spindle organization
A	0070098	biological_process	chemokine-mediated signaling pathway
A	0072678	biological_process	T cell migration
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099645	biological_process	neurotransmitter receptor localization to postsynaptic specialization membrane
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	0003925	molecular_function	G protein activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005813	cellular_component	centrosome
B	0005829	cellular_component	cytosol
B	0005834	cellular_component	heterotrimeric G-protein complex
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	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor signaling pathway
B	0010855	molecular_function	adenylate cyclase inhibitor activity
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
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	0032794	molecular_function	GTPase activating protein binding
B	0032991	cellular_component	protein-containing complex
B	0034695	biological_process	response to prostaglandin E
B	0043303	biological_process	mast cell degranulation
B	0045542	biological_process	positive regulation of cholesterol biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0050805	biological_process	negative regulation of synaptic transmission
B	0051301	biological_process	cell division
B	0060236	biological_process	regulation of mitotic spindle organization
B	0070098	biological_process	chemokine-mediated signaling pathway
B	0072678	biological_process	T cell migration
B	0098794	cellular_component	postsynapse
B	0098978	cellular_component	glutamatergic synapse
B	0099645	biological_process	neurotransmitter receptor localization to postsynaptic specialization membrane
B	1904322	biological_process	cellular response to forskolin
B	1904778	biological_process	positive regulation of protein localization to cell cortex

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP A 355

Chain	Residue
A	GLY42
A	ARG176
A	THR177
A	ARG178
A	ASN269
A	LYS270
A	ASP272
A	LEU273
A	CYS325
A	ALA326
A	THR327
A	GLU43
A	SER44
A	GLY45
A	LYS46
A	SER47
A	THR48
A	SER151
A	LEU175

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP B 355

Chain	Residue
B	ALA41
B	GLY42
B	GLU43
B	SER44
B	GLY45
B	LYS46
B	SER47
B	THR48
B	ASP150
B	SER151
B	LEU175
B	ARG176
B	THR177
B	ARG178
B	ASN269
B	LYS270
B	ASP272
B	LEU273
B	CYS325
B	ALA326
B	THR327

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	26
Details	Binding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19703466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	9
Details	Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	THR181
A	GLU43
A	ARG178

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

Chain	Residue	Details
B	THR181
B	GLN204
B	GLU43
B	ARG178

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

Chain	Residue	Details
B	GLN204

site_id	MCSA1
Number of Residues	4
Details	M-CSA 533

Chain	Residue	Details
A	GLU43	electrostatic stabiliser
A	THR48	electrostatic stabiliser
A	ARG178	electrostatic stabiliser
A	ASP200	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 533

Chain	Residue	Details
B	GLU43	electrostatic stabiliser
B	THR48	electrostatic stabiliser
B	ARG178	electrostatic stabiliser
B	ASP200	electrostatic stabiliser
B	GLN204	electrostatic stabiliser

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