2V4Z

The crystal structure of the human G-protein subunit alpha (GNAI3) in complex with an engineered regulator of G-protein signaling type 2 domain (RGS2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0000166	molecular_function	nucleotide 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	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005834	cellular_component	heterotrimeric G-protein complex
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
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	0007194	biological_process	negative regulation of adenylate cyclase activity
A	0016020	cellular_component	membrane
A	0016239	biological_process	positive regulation of macroautophagy
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	0034451	cellular_component	centriolar satellite
A	0036064	cellular_component	ciliary basal body
A	0046039	biological_process	GTP metabolic process
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division
A	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GDP A 1348

Chain	Residue
A	GLU43
A	ARG176
A	THR177
A	ARG178
A	ASN269
A	LYS270
A	ASP272
A	LEU273
A	CYS325
A	ALA326
A	THR327
A	SER44
A	ALF1349
A	MG1350
A	HOH2002
A	HOH2015
A	HOH2016
A	GLY45
A	LYS46
A	SER47
A	THR48
A	ASP150
A	SER151
A	LEU175

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ALF A 1349

Chain	Residue
A	GLY42
A	GLU43
A	LYS46
A	ARG178
A	LYS180
A	THR181
A	VAL201
A	GLY203
A	GLN204
A	GDP1348
A	MG1350
A	HOH2002
A	HOH2012
A	HOH2015

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1350

Chain	Residue
A	SER47
A	THR181
A	GDP1348
A	ALF1349
A	HOH2002
A	HOH2015

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
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	8
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	9
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	7
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	5
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	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37137991","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X6I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GVX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19478087","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IHB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ODE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V4Z","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37137991","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylarginine; by cholera toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
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_FI11
Number of Residues	37
Details	Region: {"description":"Necessary to inhibit protein synthesis","evidences":[{"source":"PubMed","id":"19736320","evidenceCode":"ECO:0000269"}]}

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	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	GLN204

---