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6RD6

CryoEM structure of Polytomella F-ATP synthase, focussed refinement of upper peripheral stalk

Functional Information from GO Data
ChainGOidnamespacecontents
P0015986biological_processproton motive force-driven ATP synthesis
P0016020cellular_componentmembrane
P0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
T0005524molecular_functionATP binding
T0005743cellular_componentmitochondrial inner membrane
T0015986biological_processproton motive force-driven ATP synthesis
T0032559molecular_functionadenyl ribonucleotide binding
T0043531molecular_functionADP binding
T0045259cellular_componentproton-transporting ATP synthase complex
T0046034biological_processATP metabolic process
T0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
T1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PALNVGLSVS
ChainResidueDetails
TPRO419-SER428

site_idPS00389
Number of Residues20
DetailsATPASE_DELTA ATP synthase delta (OSCP) subunit signature. LvMqekIDkKLlGGFVIEfS
ChainResidueDetails
PLEU184-SER203

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PDB entries from 2026-04-01

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