6RDF

CryoEM structure of Polytomella F-ATP synthase, Primary rotary state 3, monomer-masked refinement

Functional Information from GO Data

Chain	GOid	namespace	contents
0	0016020	cellular_component	membrane
1	0005739	cellular_component	mitochondrion
8	0016020	cellular_component	membrane
9	0016020	cellular_component	membrane
M	0006754	biological_process	ATP biosynthetic process
M	0006811	biological_process	monoatomic ion transport
M	0015078	molecular_function	proton transmembrane transporter activity
M	0015986	biological_process	proton motive force-driven ATP synthesis
M	0016020	cellular_component	membrane
M	0045259	cellular_component	proton-transporting ATP synthase complex
M	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
M	1902600	biological_process	proton transmembrane transport
P	0006754	biological_process	ATP biosynthetic process
P	0006811	biological_process	monoatomic ion transport
P	0015986	biological_process	proton motive force-driven ATP synthesis
P	0016020	cellular_component	membrane
P	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
P	1902600	biological_process	proton transmembrane transport
T	0000166	molecular_function	nucleotide binding
T	0005524	molecular_function	ATP binding
T	0005743	cellular_component	mitochondrial inner membrane
T	0006754	biological_process	ATP biosynthetic process
T	0006811	biological_process	monoatomic ion transport
T	0015986	biological_process	proton motive force-driven ATP synthesis
T	0016020	cellular_component	membrane
T	0016787	molecular_function	hydrolase activity
T	0032559	molecular_function	adenyl ribonucleotide binding
T	0043531	molecular_function	ADP binding
T	0045259	cellular_component	proton-transporting ATP synthase complex
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 PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ZN M 600

Chain	Residue
6	HOH202
M	HIS248
M	HIS252

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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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site_id	PS00449
Number of Residues	10
Details	ATPASE_A ATP synthase a subunit signature. SLGVRLWVNM

Chain	Residue	Details
M	SER235-MET244

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