Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UMR

Crystal structure of the G202D mutant of human G-alpha-i1

Replaces: 2EBC

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	0072678	biological_process	T cell migration
A	1904322	biological_process	cellular response to forskolin
A	1904778	biological_process	positive regulation of protein localization to cell cortex

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GDP A 400

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	HOH372
A	HOH382
A	HOH385
A	HOH386
A	HOH389
A	HOH405
A	GLY45
A	LYS46
A	SER47
A	THR48
A	ASP150
A	SER151
A	LEU175

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 355

Chain	Residue
A	ARG15
A	ARG21
A	ARG32
A	LYS180
A	LEU348
A	HOH557

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 356

Chain	Residue
A	ASN331

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 357

Chain	Residue
A	ALA121

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 359

Chain	Residue
A	GLU28
A	LYS29
A	ALA30
A	ASP193
A	HIS195
A	HOH380

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18434541, ECO:0000269\|PubMed:22383884, ECO:0007744\|PDB:3QE0

Chain	Residue	Details
A	SER47
A	THR181

site_id	SWS_FT_FI3
Number of Residues	1
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

site_id	SWS_FT_FI4
Number of Residues	1
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

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486

Chain	Residue	Details
A	ASP200

site_id	SWS_FT_FI6
Number of Residues	1
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

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
A	ARG178

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
A	GLN204

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
A	CYS351

site_id	SWS_FT_FI10
Number of Residues	1
Details	LIPID: N-myristoyl glycine => ECO:0000269\|PubMed:20213681, ECO:0000269\|PubMed:25255805

Chain	Residue	Details
A	GLY2

site_id	SWS_FT_FI11
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000250\|UniProtKB:P10824

Chain	Residue	Details
A	CYS3

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