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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2W6I

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 4B.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein 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
A0016020cellular_componentmembrane
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
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein 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
B0016020cellular_componentmembrane
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
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
C0016020cellular_componentmembrane
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
D0000166molecular_functionnucleotide binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0006754biological_processATP biosynthetic process
D0006811biological_processmonoatomic ion transport
D0015986biological_processproton motive force-driven ATP synthesis
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0042776biological_processproton motive force-driven mitochondrial ATP synthesis
D0045259cellular_componentproton-transporting ATP synthase complex
D0046034biological_processATP metabolic process
D0046872molecular_functionmetal ion binding
D0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
D1902600biological_processproton transmembrane transport
E0000166molecular_functionnucleotide binding
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005743cellular_componentmitochondrial inner membrane
E0006754biological_processATP biosynthetic process
E0006811biological_processmonoatomic ion transport
E0015986biological_processproton motive force-driven ATP synthesis
E0016020cellular_componentmembrane
E0016887molecular_functionATP hydrolysis activity
E0042776biological_processproton motive force-driven mitochondrial ATP synthesis
E0045259cellular_componentproton-transporting ATP synthase complex
E0046034biological_processATP metabolic process
E0046872molecular_functionmetal ion binding
E0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
E1902600biological_processproton transmembrane transport
F0000166molecular_functionnucleotide binding
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005743cellular_componentmitochondrial inner membrane
F0006754biological_processATP biosynthetic process
F0006811biological_processmonoatomic ion transport
F0015986biological_processproton motive force-driven ATP synthesis
F0016020cellular_componentmembrane
F0016887molecular_functionATP hydrolysis activity
F0042776biological_processproton motive force-driven mitochondrial ATP synthesis
F0045259cellular_componentproton-transporting ATP synthase complex
F0046034biological_processATP metabolic process
F0046872molecular_functionmetal ion binding
F0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
F1902600biological_processproton transmembrane transport
G0005515molecular_functionprotein binding
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0006754biological_processATP biosynthetic process
G0006811biological_processmonoatomic ion transport
G0015986biological_processproton motive force-driven ATP synthesis
G0016020cellular_componentmembrane
G0042776biological_processproton motive force-driven mitochondrial ATP synthesis
G0045259cellular_componentproton-transporting ATP synthase complex
G0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
G1902600biological_processproton transmembrane transport
H0005198molecular_functionstructural molecule activity
H0005739cellular_componentmitochondrion
H0005740cellular_componentmitochondrial envelope
H0005743cellular_componentmitochondrial inner membrane
H0006754biological_processATP biosynthetic process
H0006811biological_processmonoatomic ion transport
H0009060biological_processaerobic respiration
H0015078molecular_functionproton transmembrane transporter activity
H0015986biological_processproton motive force-driven ATP synthesis
H0016020cellular_componentmembrane
H0033615biological_processmitochondrial proton-transporting ATP synthase complex assembly
H0042776biological_processproton motive force-driven mitochondrial ATP synthesis
H0045259cellular_componentproton-transporting ATP synthase complex
H0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
H1902600biological_processproton transmembrane transport
I0005739cellular_componentmitochondrion
I0005743cellular_componentmitochondrial inner membrane
I0006754biological_processATP biosynthetic process
I0006811biological_processmonoatomic ion transport
I0015986biological_processproton motive force-driven ATP synthesis
I0016020cellular_componentmembrane
I0042776biological_processproton motive force-driven mitochondrial ATP synthesis
I0045259cellular_componentproton-transporting ATP synthase complex
I0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
I1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
ChainResidueDetails
APRO363-SER372
DPRO346-SER355
site_idPS00153
Number of Residues14
DetailsATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA
ChainResidueDetails
GILE258-ALA271
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17895376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8065448","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8790345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1COW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E1Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OHH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CK3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JIZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WSS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TSF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TT3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Z1M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues15
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues33
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","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_FI12
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17895376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H8E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ASU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TSF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues15
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10719","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG373
site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
ALYS175
ALYS209
AGLN208
site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BLYS175
BLYS209
BGLN208
site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
CLYS175
CLYS209
CGLN208
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BARG373
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
CARG373
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
DARG356
site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
EARG356
site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
FARG356
site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
DARG189
DLYS162
DGLU188
site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
EARG189
ELYS162
EGLU188
site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
FARG189
FLYS162
FGLU188
site_idMCSA1
Number of Residues3
DetailsM-CSA 178
ChainResidueDetails
DLYS162electrostatic stabiliser
DGLU188electrostatic stabiliser
DARG189electrostatic stabiliser
site_idMCSA2
Number of Residues3
DetailsM-CSA 178
ChainResidueDetails
ELYS162electrostatic stabiliser
EGLU188electrostatic stabiliser
EARG189electrostatic stabiliser
site_idMCSA3
Number of Residues3
DetailsM-CSA 178
ChainResidueDetails
FLYS162electrostatic stabiliser
FGLU188electrostatic stabiliser
FARG189electrostatic stabiliser

238895

PDB entries from 2025-07-16

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