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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2JDI

Ground state structure of F1-ATPase from bovine heart mitochondria (Bovine F1-ATPase crystallised in the absence of azide)

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
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
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 PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A1512
ChainResidue
ATHR176
AANP1511
AHOH2150
AHOH2200
AHOH2347
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B1512
ChainResidue
BHOH2345
BTHR176
BANP1511
BHOH2167
BHOH2223
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C1512
ChainResidue
CTHR176
CANP1511
CHOH2144
CHOH2192
CHOH2363
site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D1481
ChainResidue
DTHR163
DANP1480
DHOH2166
DHOH2213
DHOH2384
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F1480
ChainResidue
FTHR163
FANP1479
FHOH2218
FHOH2260
FHOH2435
site_idAC6
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ANP A1511
ChainResidue
AARG171
AGLN172
ATHR173
AGLY174
ALYS175
ATHR176
ASER177
APHE357
AGLN430
AGLN432
AMG1512
AHOH2147
AHOH2200
AHOH2347
AHOH2349
AHOH2350
AHOH2351
AHOH2352
AHOH2353
AHOH2354
AHOH2355
DTYR368
DHOH2303
DHOH2306
DHOH2307
DHOH2319
site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP B1511
ChainResidue
BARG171
BGLN172
BTHR173
BGLY174
BLYS175
BTHR176
BSER177
BPHE357
BARG362
BGLN430
BGLN432
BMG1512
BHOH2223
BHOH2281
BHOH2344
BHOH2345
BHOH2346
BHOH2347
BHOH2348
EARG356
site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ANP C1511
ChainResidue
CARG171
CGLN172
CTHR173
CGLY174
CLYS175
CTHR176
CSER177
CPHE357
CGLN430
CGLN432
CMG1512
CHOH2192
CHOH2359
CHOH2360
CHOH2361
CHOH2362
CHOH2363
CHOH2364
CHOH2365
CHOH2366
CHOH2367
FHOH2350
FHOH2351
FHOH2364
site_idAC9
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ANP D1480
ChainResidue
DGLY159
DVAL160
DGLY161
DLYS162
DTHR163
DVAL164
DGLU188
DARG189
DTYR311
DTYR345
DPHE418
DALA421
DPHE424
DTHR425
DMG1481
DHOH2166
DHOH2167
DHOH2168
DHOH2213
DHOH2384
DHOH2385
DHOH2386
DHOH2387
DHOH2388
DHOH2389
CSER344
CSER372
CARG373
DGLY157
site_idBC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ANP F1479
ChainResidue
BILE343
BSER344
BVAL371
BARG373
FGLY157
FALA158
FGLY159
FVAL160
FGLY161
FLYS162
FTHR163
FVAL164
FGLU188
FARG189
FTYR345
FPHE418
FALA421
FPHE424
FTHR425
FMG1480
FHOH2206
FHOH2260
FHOH2430
FHOH2432
FHOH2433
FHOH2434
FHOH2435
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 Residues6
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 Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D3D9","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
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
DARG356
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
EARG356
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
FARG356
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
CARG373
DARG189
DGLU188
DLYS162
site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG373
EARG189
EGLU188
ELYS162
site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
FARG189
FGLU188
FLYS162
BARG373
site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
ALYS175
ALYS209
AGLN208
site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BLYS175
BLYS209
BGLN208
site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
CLYS175
CLYS209
CGLN208
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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