1DS6

CRYSTAL STRUCTURE OF A RAC-RHOGDI COMPLEX

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003924	molecular_function	GTPase 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	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007264	biological_process	small GTPase-mediated signal transduction
A	0008283	biological_process	cell population proliferation
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	0016787	molecular_function	hydrolase activity
A	0019887	molecular_function	protein kinase regulator activity
A	0019901	molecular_function	protein kinase binding
A	0030027	cellular_component	lamellipodium
A	0030031	biological_process	cell projection assembly
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	0042995	cellular_component	cell projection
A	0043020	cellular_component	NADPH oxidase complex
A	0043131	biological_process	erythrocyte enucleation
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	0070662	biological_process	mast cell proliferation
A	0070668	biological_process	positive regulation of mast cell proliferation
A	0071593	biological_process	lymphocyte aggregation
A	0090023	biological_process	positive regulation of neutrophil chemotaxis
A	1902622	biological_process	regulation of neutrophil migration
A	1903955	biological_process	positive regulation of protein targeting to mitochondrion
B	0005094	molecular_function	Rho GDP-dissociation inhibitor activity
B	0005737	cellular_component	cytoplasm
B	0007266	biological_process	Rho protein signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 193

Chain	Residue
A	THR17
A	THR35
A	GDP194
A	HOH509
A	HOH539
A	HOH550

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GDP A 194

Chain	Residue
A	VAL14
A	GLY15
A	LYS16
A	THR17
A	CYS18
A	PHE28
A	ILE33
A	LYS116
A	ASP118
A	LEU119
A	SER158
A	ALA159
A	LEU160
A	MG193
A	HOH531
A	HOH539
A	HOH547
A	HOH550
A	HOH576
A	HOH592
A	HOH593
A	HOH628
A	ASP11
A	GLY12
A	ALA13

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
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":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylasparagine; by botulinum toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

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
A	ALA13

---