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6J5J

Cryo-EM structure of the mammalian E-state ATP synthase

Functional Information from GO Data
ChainGOidnamespacecontents
80006754biological_processATP biosynthetic process
80006811biological_processmonoatomic ion transport
80015078molecular_functionproton transmembrane transporter activity
80015986biological_processproton motive force-driven ATP synthesis
80031966cellular_componentmitochondrial membrane
80042776biological_processproton motive force-driven mitochondrial ATP synthesis
80045259cellular_componentproton-transporting ATP synthase complex
80046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
81902600biological_processproton transmembrane transport
a0005743cellular_componentmitochondrial inner membrane
a0006754biological_processATP biosynthetic process
a0006811biological_processmonoatomic ion transport
a0015078molecular_functionproton transmembrane transporter activity
a0015252molecular_functionproton channel activity
a0015986biological_processproton motive force-driven ATP synthesis
a0045259cellular_componentproton-transporting ATP synthase complex
a0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
a1902600biological_processproton transmembrane transport
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005886cellular_componentplasma membrane
A0006754biological_processATP biosynthetic process
A0006811biological_processmonoatomic ion transport
A0015986biological_processproton motive force-driven ATP synthesis
A0032559molecular_functionadenyl ribonucleotide binding
A0043531molecular_functionADP binding
A0045259cellular_componentproton-transporting ATP synthase complex
A0046034biological_processATP metabolic process
A0046872molecular_functionmetal ion binding
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
b0015078molecular_functionproton transmembrane transporter activity
b0015986biological_processproton motive force-driven ATP synthesis
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005886cellular_componentplasma membrane
B0006754biological_processATP biosynthetic process
B0006811biological_processmonoatomic ion transport
B0015986biological_processproton motive force-driven ATP synthesis
B0032559molecular_functionadenyl ribonucleotide binding
B0043531molecular_functionADP binding
B0045259cellular_componentproton-transporting ATP synthase complex
B0046034biological_processATP metabolic process
B0046872molecular_functionmetal ion binding
B0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
B1902600biological_processproton transmembrane transport
c0005739cellular_componentmitochondrion
c0005743cellular_componentmitochondrial inner membrane
c0006811biological_processmonoatomic ion transport
c0015078molecular_functionproton transmembrane transporter activity
c0015986biological_processproton motive force-driven ATP synthesis
c0045259cellular_componentproton-transporting ATP synthase complex
c1902600biological_processproton transmembrane transport
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0005886cellular_componentplasma membrane
C0006754biological_processATP biosynthetic process
C0006811biological_processmonoatomic ion transport
C0015986biological_processproton motive force-driven ATP synthesis
C0032559molecular_functionadenyl ribonucleotide binding
C0043531molecular_functionADP binding
C0045259cellular_componentproton-transporting ATP synthase complex
C0046034biological_processATP metabolic process
C0046872molecular_functionmetal ion binding
C0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
C1902600biological_processproton transmembrane transport
d0015078molecular_functionproton transmembrane transporter activity
d0015986biological_processproton motive force-driven ATP synthesis
d0045259cellular_componentproton-transporting ATP synthase complex
D0005524molecular_functionATP binding
D0015986biological_processproton motive force-driven ATP synthesis
D0045259cellular_componentproton-transporting ATP synthase complex
D0046034biological_processATP metabolic process
D0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
D1902600biological_processproton transmembrane transport
E0005524molecular_functionATP binding
E0015986biological_processproton motive force-driven ATP synthesis
E0045259cellular_componentproton-transporting ATP synthase complex
E0046034biological_processATP metabolic process
E0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
E1902600biological_processproton transmembrane transport
f0005739cellular_componentmitochondrion
f0005743cellular_componentmitochondrial inner membrane
f0006754biological_processATP biosynthetic process
f0006811biological_processmonoatomic ion transport
f0045259cellular_componentproton-transporting ATP synthase complex
f1902600biological_processproton transmembrane transport
F0005524molecular_functionATP binding
F0015986biological_processproton motive force-driven ATP synthesis
F0045259cellular_componentproton-transporting ATP synthase complex
F0046034biological_processATP metabolic process
F0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
F1902600biological_processproton transmembrane transport
G0015986biological_processproton motive force-driven ATP synthesis
G0045259cellular_componentproton-transporting ATP synthase complex
G0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
H0015986biological_processproton motive force-driven ATP synthesis
H0045259cellular_componentproton-transporting ATP synthase complex
H0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
I0005739cellular_componentmitochondrion
I0005743cellular_componentmitochondrial inner membrane
I0006754biological_processATP biosynthetic process
I0006811biological_processmonoatomic ion transport
I0015986biological_processproton motive force-driven ATP synthesis
I0045259cellular_componentproton-transporting ATP synthase complex
I0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
I1902600biological_processproton transmembrane transport
J0005739cellular_componentmitochondrion
J0032780biological_processnegative regulation of ATP-dependent activity
J0042030molecular_functionATPase inhibitor activity
K0015078molecular_functionproton transmembrane transporter activity
K0015986biological_processproton motive force-driven ATP synthesis
K0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
K0045259cellular_componentproton-transporting ATP synthase complex
K1902600biological_processproton transmembrane transport
L0015078molecular_functionproton transmembrane transporter activity
L0015986biological_processproton motive force-driven ATP synthesis
L0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
L0045259cellular_componentproton-transporting ATP synthase complex
L1902600biological_processproton transmembrane transport
M0015078molecular_functionproton transmembrane transporter activity
M0015986biological_processproton motive force-driven ATP synthesis
M0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
M0045259cellular_componentproton-transporting ATP synthase complex
M1902600biological_processproton transmembrane transport
N0015078molecular_functionproton transmembrane transporter activity
N0015986biological_processproton motive force-driven ATP synthesis
N0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
N0045259cellular_componentproton-transporting ATP synthase complex
N1902600biological_processproton transmembrane transport
O0015078molecular_functionproton transmembrane transporter activity
O0015986biological_processproton motive force-driven ATP synthesis
O0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
O0045259cellular_componentproton-transporting ATP synthase complex
O1902600biological_processproton transmembrane transport
P0015078molecular_functionproton transmembrane transporter activity
P0015986biological_processproton motive force-driven ATP synthesis
P0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
P0045259cellular_componentproton-transporting ATP synthase complex
P1902600biological_processproton transmembrane transport
Q0015078molecular_functionproton transmembrane transporter activity
Q0015986biological_processproton motive force-driven ATP synthesis
Q0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
Q0045259cellular_componentproton-transporting ATP synthase complex
Q1902600biological_processproton transmembrane transport
R0015078molecular_functionproton transmembrane transporter activity
R0015986biological_processproton motive force-driven ATP synthesis
R0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
R0045259cellular_componentproton-transporting ATP synthase complex
R1902600biological_processproton transmembrane transport
S0015986biological_processproton motive force-driven ATP synthesis
S0016020cellular_componentmembrane
S0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ATP A 601
ChainResidue
AGLN172
AMG602
DARG358
ATHR173
AGLY174
ALYS175
ATHR176
ASER177
AARG362
AGLN430
AGLN432

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 602
ChainResidue
ATHR176
AATP601

site_idAC3
Number of Residues11
Detailsbinding site for residue ATP B 601
ChainResidue
BGLN172
BTHR173
BGLY174
BLYS175
BTHR176
BSER177
BPHE357
BGLN430
BGLN432
BMG602
EASP361

site_idAC4
Number of Residues2
Detailsbinding site for residue MG B 602
ChainResidue
BTHR176
BATP601

site_idAC5
Number of Residues9
Detailsbinding site for residue ATP C 601
ChainResidue
CGLN172
CGLY174
CLYS175
CTHR176
CSER177
CARG362
CGLY431
CMG602
FMET360

site_idAC6
Number of Residues2
Detailsbinding site for residue MG C 602
ChainResidue
CTHR176
CATP601

site_idAC7
Number of Residues9
Detailsbinding site for residue ADP D 501
ChainResidue
DGLY161
DGLY163
DLYS164
DTHR165
DVAL166
DTYR347
DPHE420
DALA423
DMG502

site_idAC8
Number of Residues3
Detailsbinding site for residue MG D 502
ChainResidue
DTHR165
DGLU190
DADP501

site_idAC9
Number of Residues11
Detailsbinding site for residue ADP F 501
ChainResidue
BARG373
FGLY161
FVAL162
FGLY163
FLYS164
FTHR165
FVAL166
FTYR347
FPHE420
FPHE426
FMG502

site_idAD1
Number of Residues2
Detailsbinding site for residue MG F 502
ChainResidue
FTHR165
FADP501

Functional Information from PROSITE/UniProt
site_idPS00449
Number of Residues10
DetailsATPASE_A ATP synthase a subunit signature. ALAVRLTANI
ChainResidueDetails
aALA155-ILE164

site_idPS00153
Number of Residues14
DetailsATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA
ChainResidueDetails
GILE258-ALA271

site_idPS00389
Number of Residues20
DetailsATPASE_DELTA ATP synthase delta (OSCP) subunit signature. LkLevkVDpSImGGMIVRiG
ChainResidueDetails
SLEU148-GLY167

site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARNPslkqqLfSyaILgfaLsE
ChainResidueDetails
PALA37-GLU58

site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
ChainResidueDetails
APRO363-SER372
DPRO348-SER357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues15
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues33
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues26
DetailsRegion: {"description":"N-terminal inhibitory region","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues5
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48047","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P18859","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P21571","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues17
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P56134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P56134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"D3ZAF6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56135","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues136
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P03930","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P03930","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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