6TMI

Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, peripheral stalk model

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015078	molecular_function	proton transmembrane transporter activity
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0045259	cellular_component	proton-transporting ATP synthase complex
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0006754	biological_process	ATP biosynthetic process
C	0006811	biological_process	monoatomic ion transport
C	0015986	biological_process	proton motive force-driven ATP synthesis
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0032559	molecular_function	adenyl ribonucleotide binding
C	0043531	molecular_function	ADP binding
C	0045259	cellular_component	proton-transporting ATP synthase complex
C	0046034	biological_process	ATP metabolic process
C	0046872	molecular_function	metal ion binding
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
G	0006754	biological_process	ATP biosynthetic process
G	0006811	biological_process	monoatomic ion transport
G	0015986	biological_process	proton motive force-driven ATP synthesis
G	0016020	cellular_component	membrane
G	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
G	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. PAINVGLSVS

Chain	Residue	Details
C	PRO415-SER424

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