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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2XND

Crystal structure of bovine F1-c8 sub-complex of ATP Synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0015986biological_processproton motive force-driven ATP synthesis
A0032559molecular_functionadenyl ribonucleotide binding
A0045259cellular_componentproton-transporting ATP synthase complex
A0046034biological_processATP metabolic process
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
B0005524molecular_functionATP binding
B0015986biological_processproton motive force-driven ATP synthesis
B0032559molecular_functionadenyl ribonucleotide binding
B0045259cellular_componentproton-transporting ATP synthase complex
B0046034biological_processATP metabolic process
B0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
B1902600biological_processproton transmembrane transport
C0005524molecular_functionATP binding
C0015986biological_processproton motive force-driven ATP synthesis
C0032559molecular_functionadenyl ribonucleotide binding
C0045259cellular_componentproton-transporting ATP synthase complex
C0046034biological_processATP metabolic process
C0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
C1902600biological_processproton transmembrane transport
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
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
G0005515molecular_functionprotein binding
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0006754biological_processATP biosynthetic process
G0006811biological_processmonoatomic ion transport
G0015986biological_processproton motive force-driven ATP synthesis
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
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
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
J0015078molecular_functionproton transmembrane transporter activity
J0015986biological_processproton motive force-driven ATP synthesis
J0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
J0045259cellular_componentproton-transporting ATP synthase complex
J1902600biological_processproton transmembrane transport
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
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ANP A 600
ChainResidue
AARG171
APRO363
AGLN430
AGLN432
AMG601
AGLN172
ATHR173
AGLY174
ALYS175
ATHR176
ASER177
APHE357
AARG362
site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
ATHR176
AASP269
AANP600
site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ANP B 600
ChainResidue
BARG171
BGLN172
BTHR173
BGLY174
BLYS175
BTHR176
BSER177
BPHE357
BARG362
BGLN430
BGLN432
BMG601
EARG356
EASP359
site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BTHR176
BANP600
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 701
ChainResidue
BMET62
BVAL129
BTYR244
BTYR248
BARG304
site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ANP C 600
ChainResidue
CARG171
CGLN172
CGLY174
CLYS175
CTHR176
CSER177
CGLU328
CPHE357
CARG362
CGLN430
CGLN432
CMG601
FTYR368
site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 601
ChainResidue
CTHR176
CASP269
CANP600
site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP D 600
ChainResidue
CSER344
CSER372
CARG373
DGLY157
DALA158
DGLY159
DVAL160
DGLY161
DLYS162
DTHR163
DVAL164
DGLU188
DARG189
DTYR311
DTYR345
DALA421
DPHE424
DTHR425
DMG601
site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 601
ChainResidue
DTHR163
DGLU188
DASP256
DANP600
site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 630
ChainResidue
AARG373
ELYS162
EARG189
EASP256
EARG260
site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP F 600
ChainResidue
FMG601
BILE343
BSER344
BARG373
FGLY157
FALA158
FGLY159
FVAL160
FGLY161
FLYS162
FTHR163
FVAL164
FGLU188
FARG189
FTYR345
FPHE418
FALA421
FPHE424
FTHR425
site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 601
ChainResidue
FTHR163
FGLU188
FARG189
FGLU192
FANP600
Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS
ChainResidueDetails
DPRO346-SER355
APRO363-SER372
site_idPS00153
Number of Residues14
DetailsATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA
ChainResidueDetails
GILE258-ALA271
site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARNPslkqqLfSyaILgfaLsE
ChainResidueDetails
JALA37-GLU58
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 Residues9
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_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 Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D3D9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues320
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues8
DetailsSite: {"description":"Reversibly protonated during proton transport","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues8
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"P05496","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
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

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PDB entries from 2025-12-24

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