Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MIT

Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	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	0007165	biological_process	signal transduction
A	0007264	biological_process	small GTPase-mediated signal transduction
A	0008360	biological_process	regulation of cell shape
A	0016787	molecular_function	hydrolase activity
A	0019901	molecular_function	protein kinase binding
A	0030865	biological_process	cortical cytoskeleton organization
A	0031410	cellular_component	cytoplasmic vesicle
A	0032956	biological_process	regulation of actin cytoskeleton organization
A	0042995	cellular_component	cell projection
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
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	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	0007165	biological_process	signal transduction
B	0007264	biological_process	small GTPase-mediated signal transduction
B	0008360	biological_process	regulation of cell shape
B	0016787	molecular_function	hydrolase activity
B	0019901	molecular_function	protein kinase binding
B	0030865	biological_process	cortical cytoskeleton organization
B	0031410	cellular_component	cytoplasmic vesicle
B	0032956	biological_process	regulation of actin cytoskeleton organization
B	0042995	cellular_component	cell projection
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003924	molecular_function	GTPase activity
C	0003925	molecular_function	G protein activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005886	cellular_component	plasma membrane
C	0007015	biological_process	actin filament organization
C	0007163	biological_process	establishment or maintenance of cell polarity
C	0007165	biological_process	signal transduction
C	0007264	biological_process	small GTPase-mediated signal transduction
C	0008360	biological_process	regulation of cell shape
C	0016787	molecular_function	hydrolase activity
C	0019901	molecular_function	protein kinase binding
C	0030865	biological_process	cortical cytoskeleton organization
C	0031410	cellular_component	cytoplasmic vesicle
C	0032956	biological_process	regulation of actin cytoskeleton organization
C	0042995	cellular_component	cell projection
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003924	molecular_function	GTPase activity
D	0003925	molecular_function	G protein activity
D	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005886	cellular_component	plasma membrane
D	0007015	biological_process	actin filament organization
D	0007163	biological_process	establishment or maintenance of cell polarity
D	0007165	biological_process	signal transduction
D	0007264	biological_process	small GTPase-mediated signal transduction
D	0008360	biological_process	regulation of cell shape
D	0016787	molecular_function	hydrolase activity
D	0019901	molecular_function	protein kinase binding
D	0030865	biological_process	cortical cytoskeleton organization
D	0031410	cellular_component	cytoplasmic vesicle
D	0032956	biological_process	regulation of actin cytoskeleton organization
D	0042995	cellular_component	cell projection
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GTP A 201

Chain	Residue
A	GLY19
A	TYR39
A	PRO41
A	THR42
A	GLY67
A	LYS123
A	ASP125
A	THR126
A	SER165
A	ALA166
A	LYS167
A	ALA20
A	MG202
A	HOH305
A	HOH306
A	HOH309
A	HOH313
A	HOH317
A	VAL21
A	GLY22
A	LYS23
A	THR24
A	CYS25
A	PHE35
A	GLU37

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 202

Chain	Residue
A	THR24
A	THR42
A	GTP201
A	HOH305
A	HOH306

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 203

Chain	Residue
A	ASP72
A	HOH327
A	HOH328
A	HOH329
A	HOH356
A	HOH360

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 204

Chain	Residue
A	ALA112
A	PRO113
A	LYS114

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GTP B 201

Chain	Residue
B	ALA20
B	VAL21
B	GLY22
B	LYS23
B	THR24
B	CYS25
B	PHE35
B	GLU37
B	TYR39
B	PRO41
B	THR42
B	GLY67
B	LYS123
B	ASP125
B	THR126
B	SER165
B	ALA166
B	LYS167
B	MG202
B	HOH303
B	HOH304
B	HOH305
B	HOH307
B	HOH311
B	HOH312

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 202

Chain	Residue
B	THR24
B	THR42
B	GTP201
B	HOH303
B	HOH304

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 203

Chain	Residue
B	ASP72
B	HOH331
B	HOH332
B	HOH333
B	HOH334
B	HOH353

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 204

Chain	Residue
B	ALA112
B	LYS114

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE GTP C 201

Chain	Residue
C	HOH315
C	HOH357
C	HOH358
C	HOH360
C	HOH363
C	GLY19
C	ALA20
C	VAL21
C	GLY22
C	LYS23
C	THR24
C	CYS25
C	PHE35
C	GLU37
C	TYR39
C	PRO41
C	THR42
C	GLY67
C	LYS123
C	ASP125
C	THR126
C	SER165
C	ALA166
C	LYS167
C	MG202
C	HOH303
C	HOH304

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 202

Chain	Residue
C	THR24
C	THR42
C	GTP201
C	HOH303
C	HOH304

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 203

Chain	Residue
C	ASP72
C	HOH320
C	HOH327
C	HOH332
C	HOH341

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 204

Chain	Residue
C	ALA112
C	PRO113
C	LYS114

site_id	BC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GTP D 201

Chain	Residue
D	GLY19
D	ALA20
D	VAL21
D	GLY22
D	LYS23
D	THR24
D	CYS25
D	PHE35
D	GLU37
D	TYR39
D	PRO41
D	THR42
D	GLY67
D	LYS123
D	ASP125
D	THR126
D	SER165
D	ALA166
D	LYS167
D	MG202
D	HOH302
D	HOH313
D	HOH314
D	HOH319
D	HOH339

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 202

Chain	Residue
D	THR24
D	THR42
D	GTP201
D	HOH302
D	HOH341

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 203

Chain	Residue
D	ASP72
D	HOH303
D	HOH304
D	HOH328
D	HOH357

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 204

Chain	Residue
D	ALA112
D	PRO113
D	LYS114
D	VAL115

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Motif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"25529118","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	72
Details	Motif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"25529118","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25529118","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MIT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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