Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2W2X

Complex of Rac2 and PLCg2 spPH Domain

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005635	cellular_component	nuclear envelope
A	0005737	cellular_component	cytoplasm
A	0005741	cellular_component	mitochondrial outer membrane
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0006935	biological_process	chemotaxis
A	0007015	biological_process	actin filament organization
A	0007163	biological_process	establishment or maintenance of cell polarity
A	0007165	biological_process	signal transduction
A	0008360	biological_process	regulation of cell shape
A	0010310	biological_process	regulation of hydrogen peroxide metabolic process
A	0010592	biological_process	positive regulation of lamellipodium assembly
A	0010810	biological_process	regulation of cell-substrate adhesion
A	0016020	cellular_component	membrane
A	0019887	molecular_function	protein kinase regulator activity
A	0019901	molecular_function	protein kinase binding
A	0030027	cellular_component	lamellipodium
A	0030036	biological_process	actin cytoskeleton organization
A	0030670	cellular_component	phagocytic vesicle membrane
A	0030865	biological_process	cortical cytoskeleton organization
A	0031410	cellular_component	cytoplasmic vesicle
A	0032956	biological_process	regulation of actin cytoskeleton organization
A	0042129	biological_process	regulation of T cell proliferation
A	0042554	biological_process	superoxide anion generation
A	0043020	cellular_component	NADPH oxidase complex
A	0043304	biological_process	regulation of mast cell degranulation
A	0045453	biological_process	bone resorption
A	0045730	biological_process	respiratory burst
A	0060263	biological_process	regulation of respiratory burst
A	0060753	biological_process	regulation of mast cell chemotaxis
A	0070062	cellular_component	extracellular exosome
A	0071593	biological_process	lymphocyte aggregation
A	0090023	biological_process	positive regulation of neutrophil chemotaxis
A	1902622	biological_process	regulation of neutrophil migration
A	1903749	biological_process	positive regulation of protein localization to mitochondrion
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	0005635	cellular_component	nuclear envelope
B	0005737	cellular_component	cytoplasm
B	0005741	cellular_component	mitochondrial outer membrane
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005884	cellular_component	actin filament
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0006935	biological_process	chemotaxis
B	0007015	biological_process	actin filament organization
B	0007163	biological_process	establishment or maintenance of cell polarity
B	0007165	biological_process	signal transduction
B	0008360	biological_process	regulation of cell shape
B	0010310	biological_process	regulation of hydrogen peroxide metabolic process
B	0010592	biological_process	positive regulation of lamellipodium assembly
B	0010810	biological_process	regulation of cell-substrate adhesion
B	0016020	cellular_component	membrane
B	0019887	molecular_function	protein kinase regulator activity
B	0019901	molecular_function	protein kinase binding
B	0030027	cellular_component	lamellipodium
B	0030036	biological_process	actin cytoskeleton organization
B	0030670	cellular_component	phagocytic vesicle membrane
B	0030865	biological_process	cortical cytoskeleton organization
B	0031410	cellular_component	cytoplasmic vesicle
B	0032956	biological_process	regulation of actin cytoskeleton organization
B	0042129	biological_process	regulation of T cell proliferation
B	0042554	biological_process	superoxide anion generation
B	0043020	cellular_component	NADPH oxidase complex
B	0043304	biological_process	regulation of mast cell degranulation
B	0045453	biological_process	bone resorption
B	0045730	biological_process	respiratory burst
B	0060263	biological_process	regulation of respiratory burst
B	0060753	biological_process	regulation of mast cell chemotaxis
B	0070062	cellular_component	extracellular exosome
B	0071593	biological_process	lymphocyte aggregation
B	0090023	biological_process	positive regulation of neutrophil chemotaxis
B	1902622	biological_process	regulation of neutrophil migration
B	1903749	biological_process	positive regulation of protein localization to mitochondrion

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GSP A 1178

Chain	Residue
A	ASP11
A	PRO34
A	THR35
A	GLY60
A	LYS116
A	ASP118
A	LEU119
A	ALA159
A	LEU160
A	MG1179
A	ALA13
A	VAL14
A	GLY15
A	LYS16
A	THR17
A	CYS18
A	PHE28
A	TYR32

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GSP B 1178

Chain	Residue
B	ASP11
B	ALA13
B	VAL14
B	GLY15
B	LYS16
B	THR17
B	CYS18
B	PHE28
B	TYR32
B	THR35
B	GLY60
B	ASP118
B	LEU119
B	SER158
B	ALA159
B	LEU160
B	MG1179

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 1179

Chain	Residue
A	THR17
A	THR35
A	ASP57
A	GSP1178

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 1179

Chain	Residue
B	THR17
B	THR35
B	ASP57
B	GSP1178

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Motif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W2X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10655614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DS6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W2X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W2V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2W2X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10655614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DS6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W2X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10655614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W2T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W2X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19394299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2W2V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylasparagine; by botulinum toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLN61

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

Chain	Residue	Details
B	GLN61

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

Chain	Residue	Details
A	ALA13

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

Chain	Residue	Details
B	ALA13

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