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6TMI

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000276cellular_componentmitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
A0015078molecular_functionproton transmembrane transporter activity
A0015986biological_processproton motive force-driven ATP synthesis
C0005524molecular_functionATP binding
C0005754cellular_componentmitochondrial proton-transporting ATP synthase, catalytic core
C0006754biological_processATP biosynthetic process
C0015986biological_processproton motive force-driven ATP synthesis
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0032559molecular_functionadenyl ribonucleotide binding
C0043531molecular_functionADP binding
C0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
C0046034biological_processATP metabolic process
C0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
C1902600biological_processproton transmembrane transport
G0000274cellular_componentmitochondrial proton-transporting ATP synthase, stator stalk
G0005886cellular_componentplasma membrane
G0006754biological_processATP biosynthetic process
G0009535cellular_componentchloroplast thylakoid membrane
G0009772biological_processphotosynthetic electron transport in photosystem II
G0009773biological_processphotosynthetic electron transport in photosystem I
G0015986biological_processproton motive force-driven ATP synthesis
G0016020cellular_componentmembrane
G0042776biological_processproton motive force-driven mitochondrial ATP synthesis
G0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
G0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
G1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
ChainResidueDetails
CPRO415-SER424

221371

PDB entries from 2024-06-19

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