+
Open data
-
Basic information
Entry | Database: PDB / ID: 3fks | ||||||
---|---|---|---|---|---|---|---|
Title | Yeast F1 ATPase in the absence of bound nucleotides | ||||||
![]() | (ATP synthase subunit ...) x 5 | ||||||
![]() | HYDROLASE / ATP synthase / ATP phosphatase / F1F0 ATPase / ATP synthesis / ATP-binding / CF(1) / Hydrogen ion transport / Ion transport / Membrane / Mitochondrion / Mitochondrion inner membrane / Nucleotide-binding / Phosphoprotein / Transport | ||||||
Function / homology | ![]() : / : / : / Mitochondrial protein degradation / : / : / mitochondrial nucleoid / : / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis ...: / : / : / Mitochondrial protein degradation / : / : / mitochondrial nucleoid / : / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / mitochondrial intermembrane space / ADP binding / mitochondrial inner membrane / ATP hydrolysis activity / mitochondrion / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kabaleeswaran, V. / Symersky, J. / Shen, H. / Walker, J.E. / Leslie, A.G.W. / Mueller, D.M. | ||||||
![]() | ![]() Title: Asymmetric structure of the yeast f1 ATPase in the absence of bound nucleotides. Authors: Kabaleeswaran, V. / Shen, H. / Symersky, J. / Walker, J.E. / Leslie, A.G. / Mueller, D.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1.7 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 1.4 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1w0jS S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | Biological unit 1: Chains A,B,C,D,E,F,G,H,I. Biological unit 2: Chains J,K,L,M,N,O,P,Q,R. Biological unit 3: Chains S,T,U,V,W,X,Y,Z,1 |
-
Components
-ATP synthase subunit ... , 5 types, 27 molecules ABCJKLSTUDEFMNOVWXGPYHQZIR1
#1: Protein | Mass: 55007.402 Da / Num. of mol.: 9 / Fragment: UNP residues 36-545 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P07251, H+-transporting two-sector ATPase #2: Protein | Mass: 52009.965 Da / Num. of mol.: 9 / Fragment: UNP residues 34-511 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Tissue fraction: mitochondria / Gene: ATP2, J2041, YJR121W / Plasmid: PRS314 / Production host: ![]() ![]() References: UniProt: P00830, H+-transporting two-sector ATPase #3: Protein | Mass: 30657.160 Da / Num. of mol.: 3 / Fragment: UNP residues 34-311 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P38077, H+-transporting two-sector ATPase #4: Protein | Mass: 14565.385 Da / Num. of mol.: 3 / Fragment: UNP residues 23-160 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: Q12165, H+-transporting two-sector ATPase #5: Protein | Mass: 6618.359 Da / Num. of mol.: 3 / Fragment: UNP residues 2-62 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P21306, H+-transporting two-sector ATPase |
---|
-Non-polymers , 1 types, 15 molecules ![](data/chem/img/PO4.gif)
#6: Chemical | ChemComp-PO4 / |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.49 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.3 Details: 6.25% PEG 6000, 10% Glycerol, 4% Methanol, 0.05M Sodium acetate, 0.5mM Nickel sulfate, 2 mM Sodium pyrophosphate, 2mM Magnesium chloride, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 18, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.587→50 Å / Num. all: 134821 / Num. obs: 134821 / % possible obs: 98 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -1 / Redundancy: 2.8 % / Biso Wilson estimate: 111.6 Å2 / Rmerge(I) obs: 0.094 / Net I/σ(I): 9 |
Reflection shell | Resolution: 3.587→3.69 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.423 / Mean I/σ(I) obs: 1.6 / % possible all: 98 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB entry 1W0J Resolution: 3.587→33.203 Å / SU ML: 0.64 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 1.34 / Stereochemistry target values: MAXIMUM LIKELIHOOD
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 53.599 Å2 / ksol: 0.28 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.587→33.203 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|