2G0N

The Crystal Structure of the Human RAC3 in complex with GDP and Chloride

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	0005737	cellular_component	cytoplasm
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0007015	biological_process	actin filament organization
A	0007163	biological_process	establishment or maintenance of cell polarity
A	0007264	biological_process	small GTPase-mediated signal transduction
A	0008045	biological_process	motor neuron axon guidance
A	0008360	biological_process	regulation of cell shape
A	0010810	biological_process	regulation of cell-substrate adhesion
A	0012505	cellular_component	endomembrane system
A	0016055	biological_process	Wnt signaling pathway
A	0016601	biological_process	Rac protein signal transduction
A	0030027	cellular_component	lamellipodium
A	0030031	biological_process	cell projection assembly
A	0030036	biological_process	actin cytoskeleton organization
A	0030426	cellular_component	growth cone
A	0031410	cellular_component	cytoplasmic vesicle
A	0031941	cellular_component	filamentous actin
A	0033630	biological_process	positive regulation of cell adhesion mediated by integrin
A	0035556	biological_process	intracellular signal transduction
A	0043005	cellular_component	neuron projection
A	0043020	cellular_component	NADPH oxidase complex
A	0043025	cellular_component	neuronal cell body
A	0045730	biological_process	respiratory burst
A	0048306	molecular_function	calcium-dependent protein binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0060326	biological_process	cell chemotaxis
A	0070062	cellular_component	extracellular exosome
A	0071944	cellular_component	cell periphery
A	0098794	cellular_component	postsynapse
A	0098974	biological_process	postsynaptic actin cytoskeleton organization
A	0098978	cellular_component	glutamatergic synapse
A	0150052	biological_process	regulation of postsynapse assembly
A	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
A	1902622	biological_process	regulation of neutrophil migration
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	0005737	cellular_component	cytoplasm
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0007015	biological_process	actin filament organization
B	0007163	biological_process	establishment or maintenance of cell polarity
B	0007264	biological_process	small GTPase-mediated signal transduction
B	0008045	biological_process	motor neuron axon guidance
B	0008360	biological_process	regulation of cell shape
B	0010810	biological_process	regulation of cell-substrate adhesion
B	0012505	cellular_component	endomembrane system
B	0016055	biological_process	Wnt signaling pathway
B	0016601	biological_process	Rac protein signal transduction
B	0030027	cellular_component	lamellipodium
B	0030031	biological_process	cell projection assembly
B	0030036	biological_process	actin cytoskeleton organization
B	0030426	cellular_component	growth cone
B	0031410	cellular_component	cytoplasmic vesicle
B	0031941	cellular_component	filamentous actin
B	0033630	biological_process	positive regulation of cell adhesion mediated by integrin
B	0035556	biological_process	intracellular signal transduction
B	0043005	cellular_component	neuron projection
B	0043020	cellular_component	NADPH oxidase complex
B	0043025	cellular_component	neuronal cell body
B	0045730	biological_process	respiratory burst
B	0048306	molecular_function	calcium-dependent protein binding
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0060326	biological_process	cell chemotaxis
B	0070062	cellular_component	extracellular exosome
B	0071944	cellular_component	cell periphery
B	0098794	cellular_component	postsynapse
B	0098974	biological_process	postsynaptic actin cytoskeleton organization
B	0098978	cellular_component	glutamatergic synapse
B	0150052	biological_process	regulation of postsynapse assembly
B	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
B	1902622	biological_process	regulation of neutrophil migration

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	THR17
B	GDP502
B	HOH737
B	HOH742
B	HOH815
B	HOH818

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 602

Chain	Residue
A	HOH788
A	HOH844
A	HOH847
A	THR17
A	GDP501
A	HOH748

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL B 701

Chain	Residue
B	GLY12
B	LYS16
B	GLY60
B	GLN61
B	GDP502
B	HOH815

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 702

Chain	Residue
A	GLY12
A	LYS16
A	GLY60
A	GLN61
A	GDP501
A	HOH844

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 703

Chain	Residue
A	SER151

---

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GDP A 501

Chain	Residue
A	ALA13
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	MG602
A	CL702
A	HOH718
A	HOH727
A	HOH796
A	HOH798
A	HOH844
A	HOH847
B	TYR64

---

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDP B 502

Chain	Residue
A	TYR64
B	ALA13
B	VAL14
B	GLY15
B	LYS16
B	THR17
B	CYS18
B	PHE28
B	ILE33
B	LYS116
B	ASP118
B	LEU119
B	SER158
B	ALA159
B	LEU160
B	MG601
B	CL701
B	HOH706
B	HOH724
B	HOH742
B	HOH803
B	HOH818

---

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	4
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2005","submissionDatabase":"PDB data bank","title":"Crystal Structure of the Human Rac3 in Complex with Gdp.","authors":["Debreczeni J.E.","Yang X.","Zao Y.","Elkins J.","Gileadi C.","Burgess N.","Colebrook S.","Gileadi O.","Fedorov O.","Bunkoczi G.","von Delft F.","Doyle D.","Sundstrom M.","Arrowsmith C.","Weigelt J.","Edwards A."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"The Crystal Structure of the Human RAC3 in complex with GDP and Chloride.","authors":["Ugochukwu E.","Yang X.","Zao Y.","Elkins J.","Gileadi C.","Burgess N.","Colebrook S.","Gileadi O.","Fedorov O.","Bunkoczi G.","Sundstrom M.","Arrowsmith C.","Weigelt J.","Edwards A.","von Delft F.","Doyle D."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAC3 grown in the presence of Gpp(NH)p.","authors":["Yang X.","Ugochukwu E.","Elkins J.","Doyle D."]}},{"source":"PDB","id":"2C2H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IC5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4).","authors":["Ugochukwu E.","Yang X.","Elkins J.M.","Burgess-Brown N.","Knapp S.","Doyle D.A."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 1 (PAK1).","authors":["Ugochukwu E.","Yang X.","Elkins J.M.","Burgess-Brown N.","Bunkoczi G.","Knapp S.","Doyle D."]}},{"source":"PDB","id":"2OV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QME","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2005","submissionDatabase":"PDB data bank","title":"Crystal Structure of the Human Rac3 in Complex with Gdp.","authors":["Debreczeni J.E.","Yang X.","Zao Y.","Elkins J.","Gileadi C.","Burgess N.","Colebrook S.","Gileadi O.","Fedorov O.","Bunkoczi G.","von Delft F.","Doyle D.","Sundstrom M.","Arrowsmith C.","Weigelt J.","Edwards A."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"PDB data bank","title":"The Crystal Structure of the Human RAC3 in complex with GDP and Chloride.","authors":["Ugochukwu E.","Yang X.","Zao Y.","Elkins J.","Gileadi C.","Burgess N.","Colebrook S.","Gileadi O.","Fedorov O.","Bunkoczi G.","Sundstrom M.","Arrowsmith C.","Weigelt J.","Edwards A.","von Delft F.","Doyle D."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAC3 grown in the presence of Gpp(NH)p.","authors":["Yang X.","Ugochukwu E.","Elkins J.","Doyle D."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4).","authors":["Ugochukwu E.","Yang X.","Elkins J.M.","Burgess-Brown N.","Knapp S.","Doyle D.A."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 1 (PAK1).","authors":["Ugochukwu E.","Yang X.","Elkins J.M.","Burgess-Brown N.","Bunkoczi G.","Knapp S.","Doyle D."]}},{"source":"PDB","id":"2C2H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QME","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 4 (PAK4).","authors":["Ugochukwu E.","Yang X.","Elkins J.M.","Burgess-Brown N.","Knapp S.","Doyle D.A."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the human RAC3 in complex with the CRIB domain of human p21-activated kinase 1 (PAK1).","authors":["Ugochukwu E.","Yang X.","Elkins J.M.","Burgess-Brown N.","Bunkoczi G.","Knapp S.","Doyle D."]}},{"source":"PDB","id":"2OV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QME","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2005","submissionDatabase":"PDB data bank","title":"Crystal Structure of the Human Rac3 in Complex with Gdp.","authors":["Debreczeni J.E.","Yang X.","Zao Y.","Elkins J.","Gileadi C.","Burgess N.","Colebrook S.","Gileadi O.","Fedorov O.","Bunkoczi G.","von Delft F.","Doyle D.","Sundstrom M.","Arrowsmith C.","Weigelt J.","Edwards A."]}},{"source":"PDB","id":"2C2H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
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

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"24684802","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

---