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6YO0

Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1/peripheral stalk

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A10000166molecular_functionnucleotide binding
A10005524molecular_functionATP binding
A10006754biological_processATP biosynthetic process
A10006811biological_processmonoatomic ion transport
A10015986biological_processproton motive force-driven ATP synthesis
A10016020cellular_componentmembrane
A10032559molecular_functionadenyl ribonucleotide binding
A10043531molecular_functionADP binding
A10045259cellular_componentproton-transporting ATP synthase complex
A10046034biological_processATP metabolic process
A10046872molecular_functionmetal ion binding
A10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A11902600biological_processproton transmembrane transport
B10000166molecular_functionnucleotide binding
B10005524molecular_functionATP binding
B10006754biological_processATP biosynthetic process
B10006811biological_processmonoatomic ion transport
B10015986biological_processproton motive force-driven ATP synthesis
B10016020cellular_componentmembrane
B10032559molecular_functionadenyl ribonucleotide binding
B10043531molecular_functionADP binding
B10045259cellular_componentproton-transporting ATP synthase complex
B10046034biological_processATP metabolic process
B10046872molecular_functionmetal ion binding
B10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
B11902600biological_processproton transmembrane transport
C10000166molecular_functionnucleotide binding
C10005524molecular_functionATP binding
C10006754biological_processATP biosynthetic process
C10006811biological_processmonoatomic ion transport
C10015986biological_processproton motive force-driven ATP synthesis
C10016020cellular_componentmembrane
C10032559molecular_functionadenyl ribonucleotide binding
C10043531molecular_functionADP binding
C10045259cellular_componentproton-transporting ATP synthase complex
C10046034biological_processATP metabolic process
C10046872molecular_functionmetal ion binding
C10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
C11902600biological_processproton transmembrane transport
d0005743cellular_componentmitochondrial inner membrane
d0006811biological_processmonoatomic ion transport
d0015078molecular_functionproton transmembrane transporter activity
d0015986biological_processproton motive force-driven ATP synthesis
d0045259cellular_componentproton-transporting ATP synthase complex
d1902600biological_processproton transmembrane transport
D10000166molecular_functionnucleotide binding
D10005524molecular_functionATP binding
D10005743cellular_componentmitochondrial inner membrane
D10006754biological_processATP biosynthetic process
D10006811biological_processmonoatomic ion transport
D10015986biological_processproton motive force-driven ATP synthesis
D10016020cellular_componentmembrane
D10042776biological_processproton motive force-driven mitochondrial ATP synthesis
D10045259cellular_componentproton-transporting ATP synthase complex
D10046034biological_processATP metabolic process
D10046872molecular_functionmetal ion binding
D10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
D11902600biological_processproton transmembrane transport
E10000166molecular_functionnucleotide binding
E10005524molecular_functionATP binding
E10005743cellular_componentmitochondrial inner membrane
E10006754biological_processATP biosynthetic process
E10006811biological_processmonoatomic ion transport
E10015986biological_processproton motive force-driven ATP synthesis
E10016020cellular_componentmembrane
E10042776biological_processproton motive force-driven mitochondrial ATP synthesis
E10045259cellular_componentproton-transporting ATP synthase complex
E10046034biological_processATP metabolic process
E10046872molecular_functionmetal ion binding
E10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
E11902600biological_processproton transmembrane transport
F10000166molecular_functionnucleotide binding
F10005524molecular_functionATP binding
F10005743cellular_componentmitochondrial inner membrane
F10006754biological_processATP biosynthetic process
F10006811biological_processmonoatomic ion transport
F10015986biological_processproton motive force-driven ATP synthesis
F10016020cellular_componentmembrane
F10042776biological_processproton motive force-driven mitochondrial ATP synthesis
F10045259cellular_componentproton-transporting ATP synthase complex
F10046034biological_processATP metabolic process
F10046872molecular_functionmetal ion binding
F10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
F11902600biological_processproton transmembrane transport
g10006754biological_processATP biosynthetic process
g10006811biological_processmonoatomic ion transport
g10015986biological_processproton motive force-driven ATP synthesis
g10016020cellular_componentmembrane
g10045259cellular_componentproton-transporting ATP synthase complex
g10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
g11902600biological_processproton transmembrane transport
G10006754biological_processATP biosynthetic process
G10006811biological_processmonoatomic ion transport
G10015986biological_processproton motive force-driven ATP synthesis
G10016020cellular_componentmembrane
G10046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
G11902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ATP C1 900
ChainResidue
C1GLN203
C1GLN463
C1MG1001
C1THR204
C1GLY205
C1LYS206
C1THR207
C1ALA208
C1PHE388
C1ARG393
C1GLN461

site_idAC2
Number of Residues2
Detailsbinding site for residue MG C1 1001
ChainResidue
C1THR207
C1ATP900

site_idAC3
Number of Residues14
Detailsbinding site for residue ADP D1 900
ChainResidue
A1VAL402
A1ARG404
D1GLY176
D1GLY178
D1GLY180
D1LYS181
D1THR182
D1VAL183
D1GLU207
D1ARG208
D1TYR364
D1SER440
D1PHE443
D1MG1001

site_idAC4
Number of Residues4
Detailsbinding site for residue MG D1 1001
ChainResidue
D1THR182
D1GLU207
D1GLU211
D1ADP900

site_idAC5
Number of Residues15
Detailsbinding site for residue ATP B1 900
ChainResidue
B1ARG202
B1GLN203
B1THR204
B1GLY205
B1LYS206
B1THR207
B1ALA208
B1PHE388
B1ARG393
B1GLN461
B1ASN462
B1GLN463
B1MG1001
F1ARG375
F1ASP378

site_idAC6
Number of Residues2
Detailsbinding site for residue MG B1 1001
ChainResidue
B1THR207
B1ATP900

site_idAC7
Number of Residues12
Detailsbinding site for residue ATP A1 900
ChainResidue
A1ARG202
A1GLN203
A1GLY205
A1LYS206
A1THR207
A1ALA208
A1PHE388
A1GLN461
A1ASN462
A1GLN463
A1MG1001
E1TYR387

site_idAC8
Number of Residues2
Detailsbinding site for residue MG A1 1001
ChainResidue
A1THR207
A1ATP900

site_idAC9
Number of Residues12
Detailsbinding site for residue ADP E1 900
ChainResidue
B1VAL402
B1ARG404
E1GLY178
E1VAL179
E1GLY180
E1LYS181
E1THR182
E1VAL183
E1TYR364
E1PHE437
E1SER440
E1MG1001

site_idAD1
Number of Residues2
Detailsbinding site for residue MG E1 1001
ChainResidue
E1THR182
E1ADP900

Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS
ChainResidueDetails
D1PRO365-SER374
C1PRO394-SER403

246704

PDB entries from 2025-12-24

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