5A51

The crystal structure of Arabidopsis thaliana CAR4 in complex with two calcium ions and phophatidyl serine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005096	molecular_function	GTPase activator activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005543	molecular_function	phospholipid binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006952	biological_process	defense response
A	0008289	molecular_function	lipid binding
A	0009651	biological_process	response to salt stress
A	0009738	biological_process	abscisic acid-activated signaling pathway
A	0009789	biological_process	positive regulation of abscisic acid-activated signaling pathway
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	1900426	biological_process	positive regulation of defense response to bacterium
A	1901002	biological_process	positive regulation of response to salt stress
B	0005096	molecular_function	GTPase activator activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005543	molecular_function	phospholipid binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006952	biological_process	defense response
B	0008289	molecular_function	lipid binding
B	0009651	biological_process	response to salt stress
B	0009738	biological_process	abscisic acid-activated signaling pathway
B	0009789	biological_process	positive regulation of abscisic acid-activated signaling pathway
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	1900426	biological_process	positive regulation of defense response to bacterium
B	1901002	biological_process	positive regulation of response to salt stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1195

Chain	Residue
B	ASP51
B	ASP56
B	ASP102
B	HIS103
B	ASP104
B	HOH2048

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 1195

Chain	Residue
A	ASP104
A	HOH2034
A	HOH2035
A	HOH2161
A	ARG50
A	ASP51
A	ASP102

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1196

Chain	Residue
B	ARG50
B	ASP51
B	ASP102
B	ASP104
B	ASP110
B	HOH2042

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1196

Chain	Residue
A	ASP51
A	ASP56
A	ASP102
A	HIS103
A	ASP104
A	HOH2040

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site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SEP B 1197

Chain	Residue
A	HIS103
A	MET105
A	HOH2163
B	TYR58
B	LYS67
B	LYS69
B	TYR101
B	LYS108
B	ASP109
B	HOH2159

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:25465408, ECO:0007744|PDB:4V29

Chain	Residue	Details
A	ARG50
B	ASP56
B	ASP102
B	HIS103
B	ASP104
B	ASP110
A	ASP51
A	ASP56
A	ASP102
A	HIS103
A	ASP104
A	ASP110
B	ARG50
B	ASP51

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