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1FX0

Crystal structure of the chloroplast F1-ATPase from spinach

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006754biological_processATP biosynthetic process
A0009507cellular_componentchloroplast
A0009535cellular_componentchloroplast thylakoid membrane
A0009579cellular_componentthylakoid
A0015986biological_processproton motive force-driven ATP synthesis
A0016020cellular_componentmembrane
A0032559molecular_functionadenyl ribonucleotide binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0043531molecular_functionADP binding
A0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
A0046034biological_processATP metabolic process
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0006754biological_processATP biosynthetic process
B0009507cellular_componentchloroplast
B0009535cellular_componentchloroplast thylakoid membrane
B0009579cellular_componentthylakoid
B0015986biological_processproton motive force-driven ATP synthesis
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042776biological_processproton motive force-driven mitochondrial ATP synthesis
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
B1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS
ChainResidueDetails
BPRO363-SER372
APRO356-SER365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01347
ChainResidueDetails
BGLY172

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Required for activity => ECO:0000255|HAMAP-Rule:MF_01346
ChainResidueDetails
ASER363

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AARG366

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BGLU204
BLYS178
BARG205

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BMET374

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
AGLN201
ALYS202
ALYS176

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ohh
ChainResidueDetails
BTHR373

225946

PDB entries from 2024-10-09

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