6RD6

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

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0005739	cellular_component	mitochondrion
P	0006754	biological_process	ATP biosynthetic process
P	0015986	biological_process	proton motive force-driven ATP synthesis
P	0016020	cellular_component	membrane
P	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
P	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
P	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
P	1902600	biological_process	proton transmembrane transport
T	0005524	molecular_function	ATP binding
T	0005739	cellular_component	mitochondrion
T	0005743	cellular_component	mitochondrial inner membrane
T	0006754	biological_process	ATP biosynthetic process
T	0015986	biological_process	proton motive force-driven ATP synthesis
T	0016787	molecular_function	hydrolase activity
T	0032559	molecular_function	adenyl ribonucleotide binding
T	0043531	molecular_function	ADP binding
T	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
T	0046034	biological_process	ATP metabolic process
T	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
T	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. PALNVGLSVS

Chain	Residue	Details
T	PRO419-SER428

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site_id	PS00389
Number of Residues	20
Details	ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. LvMqekIDkKLlGGFVIEfS

Chain	Residue	Details
P	LEU184-SER203

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