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6ZIT

bovine ATP synthase Stator domain, state 2

Functional Information from GO Data
ChainGOidnamespacecontents
80005739cellular_componentmitochondrion
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
a0042776biological_processproton motive force-driven mitochondrial ATP synthesis
a0045259cellular_componentproton-transporting ATP synthase complex
a0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
a1902600biological_processproton transmembrane transport
b0015078molecular_functionproton transmembrane transporter activity
b0015986biological_processproton motive force-driven ATP synthesis
C0000166molecular_functionnucleotide binding
C0005515molecular_functionprotein 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
d0005739cellular_componentmitochondrion
d0005743cellular_componentmitochondrial inner membrane
d0006811biological_processmonoatomic ion transport
d0015078molecular_functionproton transmembrane transporter activity
d0015986biological_processproton motive force-driven ATP synthesis
d0042776biological_processproton motive force-driven mitochondrial ATP synthesis
d0045259cellular_componentproton-transporting ATP synthase complex
d0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
d1902600biological_processproton transmembrane transport
e0005739cellular_componentmitochondrion
e0005743cellular_componentmitochondrial inner membrane
e0006754biological_processATP biosynthetic process
e0006811biological_processmonoatomic ion transport
e0015078molecular_functionproton transmembrane transporter activity
e0015986biological_processproton motive force-driven ATP synthesis
e0016020cellular_componentmembrane
e0042776biological_processproton motive force-driven mitochondrial ATP synthesis
e0045259cellular_componentproton-transporting ATP synthase complex
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
f0042776biological_processproton motive force-driven mitochondrial ATP synthesis
f0045259cellular_componentproton-transporting ATP synthase complex
f0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
f1902600biological_processproton transmembrane transport
g0005739cellular_componentmitochondrion
g0005743cellular_componentmitochondrial inner membrane
g0006754biological_processATP biosynthetic process
g0006811biological_processmonoatomic ion transport
g0015078molecular_functionproton transmembrane transporter activity
g0015986biological_processproton motive force-driven ATP synthesis
g0045259cellular_componentproton-transporting ATP synthase complex
g0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
g1902600biological_processproton transmembrane transport
h0015078molecular_functionproton transmembrane transporter activity
h0015986biological_processproton motive force-driven ATP synthesis
h0045259cellular_componentproton-transporting ATP synthase complex
j0005739cellular_componentmitochondrion
j0031966cellular_componentmitochondrial membrane
j0045259cellular_componentproton-transporting ATP synthase complex
k0005739cellular_componentmitochondrion
k0031966cellular_componentmitochondrial membrane
k0045259cellular_componentproton-transporting ATP synthase complex
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
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 PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
ChainResidueDetails
CPRO363-SER372

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

site_idPS00449
Number of Residues10
DetailsATPASE_A ATP synthase a subunit signature. ALAVRLTANI
ChainResidueDetails
aALA155-ILE164

site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARNPslkqqLfSyaILgfaLsE
ChainResidueDetails
RALA37-GLU58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues198
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1827992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2875870","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"2875870","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCX2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DCX2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75947","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q06185","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues17
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P56134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56135","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75964","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPQ8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues17
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P56378","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; partial","evidences":[{"source":"UniProtKB","id":"Q78IK2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues3
DetailsSite: {"description":"Reversibly protonated during proton transport","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"Q06055","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQQ7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQQ7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P24539","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P18859","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","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":"Q9DB20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48047","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 178
ChainResidueDetails

246704

PDB entries from 2025-12-24

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