Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6RDA

CryoEM structure of Polytomella F-ATP synthase, Primary rotary state 1, monomer-masked refinement

Functional Information from GO Data
ChainGOidnamespacecontents
00016020cellular_componentmembrane
10005739cellular_componentmitochondrion
80016020cellular_componentmembrane
90016020cellular_componentmembrane
M0006754biological_processATP biosynthetic process
M0015078molecular_functionproton transmembrane transporter activity
M0015986biological_processproton motive force-driven ATP synthesis
M0016020cellular_componentmembrane
M0045259cellular_componentproton-transporting ATP synthase complex
M0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
M0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
M1902600biological_processproton transmembrane transport
P0006754biological_processATP biosynthetic process
P0015986biological_processproton motive force-driven ATP synthesis
P0016020cellular_componentmembrane
P0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
P1902600biological_processproton transmembrane transport
T0005524molecular_functionATP binding
T0005743cellular_componentmitochondrial inner membrane
T0006754biological_processATP biosynthetic process
T0015986biological_processproton motive force-driven ATP synthesis
T0016787molecular_functionhydrolase activity
T0032559molecular_functionadenyl ribonucleotide binding
T0043531molecular_functionADP binding
T0045261cellular_componentproton-transporting ATP synthase complex, catalytic core F(1)
T0046034biological_processATP metabolic process
T0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
T1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN M 600
ChainResidue
6HOH205
MHIS248
MHIS252
MHOH709

Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PALNVGLSVS
ChainResidueDetails
TPRO419-SER428

site_idPS00389
Number of Residues20
DetailsATPASE_DELTA ATP synthase delta (OSCP) subunit signature. LvMqekIDkKLlGGFVIEfS
ChainResidueDetails
PLEU184-SER203

site_idPS00449
Number of Residues10
DetailsATPASE_A ATP synthase a subunit signature. SLGVRLWVNM
ChainResidueDetails
MSER235-MET244

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon