7DQE

Crystal structure of the ADP-bound mutant A(S23C)3B(N64C)3 complex from enterococcus hirae V-ATPase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006814	biological_process	sodium ion transport
A	0035725	biological_process	sodium ion transmembrane transport
A	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
A	0045259	cellular_component	proton-transporting ATP synthase complex
A	0046034	biological_process	ATP metabolic process
A	0046932	molecular_function	sodium-transporting ATP synthase activity, rotational mechanism
A	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
A	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
A	0046962	molecular_function	sodium-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	0006814	biological_process	sodium ion transport
B	0035725	biological_process	sodium ion transmembrane transport
B	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
B	0045259	cellular_component	proton-transporting ATP synthase complex
B	0046034	biological_process	ATP metabolic process
B	0046932	molecular_function	sodium-transporting ATP synthase activity, rotational mechanism
B	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
B	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
B	0046962	molecular_function	sodium-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	0006814	biological_process	sodium ion transport
C	0035725	biological_process	sodium ion transmembrane transport
C	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
C	0045259	cellular_component	proton-transporting ATP synthase complex
C	0046034	biological_process	ATP metabolic process
C	0046932	molecular_function	sodium-transporting ATP synthase activity, rotational mechanism
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
C	0046962	molecular_function	sodium-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	0006814	biological_process	sodium ion transport
D	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
D	0046034	biological_process	ATP metabolic process
D	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006814	biological_process	sodium ion transport
E	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
E	0046034	biological_process	ATP metabolic process
E	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
E	1902600	biological_process	proton transmembrane transport
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0006814	biological_process	sodium ion transport
F	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
F	0046034	biological_process	ATP metabolic process
F	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	PRO340-SER349
A	PRO426-SER435

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY232
B	GLY232
C	GLY232

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