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2F43

Rat liver F1-ATPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000275cellular_componentmitochondrial proton-transporting ATP synthase complex, catalytic sector F(1)
A0001937biological_processnegative regulation of endothelial cell proliferation
A0002020molecular_functionprotease binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005753cellular_componentmitochondrial proton-transporting ATP synthase complex
A0005754cellular_componentmitochondrial proton-transporting ATP synthase, catalytic core
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006754biological_processATP biosynthetic process
A0008180cellular_componentCOP9 signalosome
A0009986cellular_componentcell surface
A0014850biological_processresponse to muscle activity
A0015986biological_processproton motive force-driven ATP synthesis
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0032559molecular_functionadenyl ribonucleotide binding
A0042288molecular_functionMHC class I protein binding
A0042776biological_processproton motive force-driven mitochondrial ATP synthesis
A0043531molecular_functionADP binding
A0043532molecular_functionangiostatin binding
A0043536biological_processpositive regulation of blood vessel endothelial cell migration
A0045121cellular_componentmembrane raft
A0045259cellular_componentproton-transporting ATP synthase complex
A0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
A0045471biological_processresponse to ethanol
A0046034biological_processATP metabolic process
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A0071549biological_processcellular response to dexamethasone stimulus
A0071732biological_processcellular response to nitric oxide
A1902600biological_processproton transmembrane transport
B0000275cellular_componentmitochondrial proton-transporting ATP synthase complex, catalytic sector F(1)
B0001525biological_processangiogenesis
B0001889biological_processliver development
B0005509molecular_functioncalcium ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005753cellular_componentmitochondrial proton-transporting ATP synthase complex
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006754biological_processATP biosynthetic process
B0006898biological_processreceptor-mediated endocytosis
B0006933biological_processnegative regulation of cell adhesion involved in substrate-bound cell migration
B0009631biological_processcold acclimation
B0009986cellular_componentcell surface
B0010042biological_processresponse to manganese ion
B0015986biological_processproton motive force-driven ATP synthesis
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0030228molecular_functionlipoprotein particle receptor activity
B0031966cellular_componentmitochondrial membrane
B0042288molecular_functionMHC class I protein binding
B0042645cellular_componentmitochondrial nucleoid
B0042776biological_processproton motive force-driven mitochondrial ATP synthesis
B0043531molecular_functionADP binding
B0043532molecular_functionangiostatin binding
B0043536biological_processpositive regulation of blood vessel endothelial cell migration
B0045121cellular_componentmembrane raft
B0045259cellular_componentproton-transporting ATP synthase complex
B0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
B0046034biological_processATP metabolic process
B0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
B0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
B0051453biological_processregulation of intracellular pH
B0098761biological_processcellular response to interleukin-7
B1901653biological_processcellular response to peptide
B1902600biological_processproton transmembrane transport
B1904643biological_processresponse to curcumin
B1905242biological_processresponse to 3,3',5-triiodo-L-thyronine
G0000275cellular_componentmitochondrial proton-transporting ATP synthase complex, catalytic sector F(1)
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0005753cellular_componentmitochondrial proton-transporting ATP synthase complex
G0006754biological_processATP biosynthetic process
G0015986biological_processproton motive force-driven ATP synthesis
G0016887molecular_functionATP hydrolysis activity
G0042776biological_processproton motive force-driven mitochondrial ATP synthesis
G0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
G0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
G0071732biological_processcellular response to nitric oxide
G1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VO4 B 601
ChainResidue
ASER344
BALA158
BGLY159
BLYS162
BGLU188
BARG189
BTYR311
BADP604
BMG605

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 602
ChainResidue
ATHR176
AGLN208
AASP269
AATP603

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 605
ChainResidue
BTHR163
BGLU188
BARG189
BVO4601
BADP604

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP A 603
ChainResidue
AGLN172
ATHR173
AGLY174
ALYS175
ATHR176
ASER177
AARG362
AGLY431
AGLN432
AMG602
BSER355
BASP359

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 604
ChainResidue
AVAL371
AARG373
BGLY159
BGLY161
BLYS162
BTHR163
BVAL164
BARG189
BTYR345
BPHE418
BALA421
BPHE424
BVO4601
BMG605

Functional Information from PROSITE/UniProt
site_idPS00153
Number of Residues14
DetailsATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA
ChainResidueDetails
GILE258-ALA271

site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
ChainResidueDetails
APRO363-SER372
BPRO346-SER355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
ChainResidueDetails
GLYS14
GLYS113

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2
ChainResidueDetails
GLYS24
GLYS245
BLYS111
BLYS209
BLYS214
BLYS472

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P36542
ChainResidueDetails
GLYS30
GLYS172
ASER123
ASER141

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
ChainResidueDetails
GLYS90
GLYS129

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P36542
ChainResidueDetails
GSER121

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
BSER383
BSER479
ALYS89
ALYS197
ALYS498

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P56480
ChainResidueDetails
BLYS430
BLYS435

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:24098488
ChainResidueDetails
BSER56
ALYS488
ALYS496
ALYS124
ALYS187
ALYS196
ALYS218
ALYS262
ALYS384
ALYS455
ALYS463

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
ChainResidueDetails
AARG161

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P25705
ChainResidueDetails
ALYS391

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000269|PubMed:24098488
ChainResidueDetails
ASER33

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BARG356

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG373
BARG189
BGLU188
BLYS162

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
ALYS175
ALYS209
AGLN208

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PDB entries from 2024-05-01

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