Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NJP

Structure of the assembled ATPase EscN in complex with its central stalk EscO from the enteropathogenic E. coli (EPEC) type III secretion system

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006754	biological_process	ATP biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0015031	biological_process	protein transport
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0016887	molecular_function	ATP hydrolysis activity
A	0030254	biological_process	protein secretion by the type III secretion system
A	0030257	cellular_component	type III protein secretion system complex
A	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
A	0046872	molecular_function	metal ion binding
A	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
A	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
A	1902600	biological_process	proton transmembrane transport
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006754	biological_process	ATP biosynthetic process
B	0009058	biological_process	biosynthetic process
B	0015031	biological_process	protein transport
B	0015986	biological_process	proton motive force-driven ATP synthesis
B	0016887	molecular_function	ATP hydrolysis activity
B	0030254	biological_process	protein secretion by the type III secretion system
B	0030257	cellular_component	type III protein secretion system complex
B	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
B	0046872	molecular_function	metal ion binding
B	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
B	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
B	1902600	biological_process	proton transmembrane transport
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006754	biological_process	ATP biosynthetic process
C	0009058	biological_process	biosynthetic process
C	0015031	biological_process	protein transport
C	0015986	biological_process	proton motive force-driven ATP synthesis
C	0016887	molecular_function	ATP hydrolysis activity
C	0030254	biological_process	protein secretion by the type III secretion system
C	0030257	cellular_component	type III protein secretion system complex
C	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
C	0046872	molecular_function	metal ion binding
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006754	biological_process	ATP biosynthetic process
D	0009058	biological_process	biosynthetic process
D	0015031	biological_process	protein transport
D	0015986	biological_process	proton motive force-driven ATP synthesis
D	0016887	molecular_function	ATP hydrolysis activity
D	0030254	biological_process	protein secretion by the type III secretion system
D	0030257	cellular_component	type III protein secretion system complex
D	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
D	0046872	molecular_function	metal ion binding
D	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
D	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006754	biological_process	ATP biosynthetic process
E	0009058	biological_process	biosynthetic process
E	0015031	biological_process	protein transport
E	0015986	biological_process	proton motive force-driven ATP synthesis
E	0016887	molecular_function	ATP hydrolysis activity
E	0030254	biological_process	protein secretion by the type III secretion system
E	0030257	cellular_component	type III protein secretion system complex
E	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
E	0046872	molecular_function	metal ion binding
E	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
E	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
E	1902600	biological_process	proton transmembrane transport
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006754	biological_process	ATP biosynthetic process
F	0009058	biological_process	biosynthetic process
F	0015031	biological_process	protein transport
F	0015986	biological_process	proton motive force-driven ATP synthesis
F	0016887	molecular_function	ATP hydrolysis activity
F	0030254	biological_process	protein secretion by the type III secretion system
F	0030257	cellular_component	type III protein secretion system complex
F	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
F	0046872	molecular_function	metal ion binding
F	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
F	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport
G	0005515	molecular_function	protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue ADP B 600

Chain	Residue
A	SER365
B	PHE355
B	MG601
B	AF3602
B	HOH1004
A	ARG366
B	GLY180
B	VAL181
B	GLY182
B	LYS183
B	SER184
B	THR185
B	MET189

site_id	AC2
Number of Residues	5
Details	binding site for residue MG B 601

Chain	Residue
B	SER184
B	ADP600
B	AF3602
B	HOH1001
B	HOH1002

site_id	AC3
Number of Residues	10
Details	binding site for residue AF3 B 602

Chain	Residue
A	ARG336
A	SER337
A	ARG366
B	LYS183
B	ARG207
B	LEU321
B	ADP600
B	MG601
B	HOH1001
B	HOH1003

site_id	AC4
Number of Residues	13
Details	binding site for residue ADP C 600

Chain	Residue
B	SER365
B	ARG366
C	GLY180
C	GLY182
C	LYS183
C	SER184
C	THR185
C	PHE355
C	THR428
C	MG601
C	AF3602
C	HOH1001
C	HOH1004

site_id	AC5
Number of Residues	6
Details	binding site for residue MG C 601

Chain	Residue
C	SER184
C	GLU210
C	ADP600
C	AF3602
C	HOH1001
C	HOH1002

site_id	AC6
Number of Residues	7
Details	binding site for residue AF3 C 602

Chain	Residue
B	SER337
B	ARG366
C	LYS183
C	ARG207
C	ADP600
C	MG601
C	HOH1003

site_id	AC7
Number of Residues	12
Details	binding site for residue ADP D 600

Chain	Residue
C	ARG366
D	GLY180
D	VAL181
D	GLY182
D	LYS183
D	SER184
D	THR185
D	PHE355
D	THR428
D	MG601
D	AF3602
D	HOH1001

site_id	AC8
Number of Residues	6
Details	binding site for residue MG D 601

Chain	Residue
D	SER184
D	GLU210
D	ADP600
D	AF3602
D	HOH1001
D	HOH1002

site_id	AC9
Number of Residues	11
Details	binding site for residue AF3 D 602

Chain	Residue
C	ARG336
C	SER337
C	ARG366
D	SER179
D	GLY180
D	LYS183
D	ARG207
D	LEU321
D	ADP600
D	MG601
D	HOH1003

site_id	AD1
Number of Residues	11
Details	binding site for residue ADP E 600

Chain	Residue
D	ARG366
E	GLY180
E	VAL181
E	GLY182
E	LYS183
E	SER184
E	THR185
E	PHE355
E	MG601
E	AF3602
E	HOH1004

site_id	AD2
Number of Residues	5
Details	binding site for residue MG E 601

Chain	Residue
E	SER184
E	ADP600
E	AF3602
E	HOH1001
E	HOH1002

site_id	AD3
Number of Residues	10
Details	binding site for residue AF3 E 602

Chain	Residue
D	SER337
D	ARG366
E	GLY180
E	LYS183
E	GLU206
E	ARG207
E	LEU321
E	ADP600
E	MG601
E	HOH1003

Functional Information from PROSITE/UniProt

site_id	PS00152
Number of Residues	10
Details	ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAIDIGLSAS

Chain	Residue	Details
A	PRO356-SER365

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)