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- PDB-1nbm: THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHL... -
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Basic information
Entry | Database: PDB / ID: 1nbm | ||||||
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Title | THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN | ||||||
![]() | (F1-ATPASE) x 4 | ||||||
![]() | ATP SYNTHASE / F1FO ATP SYNTHASE / F1-ATPASE / 4-CHLORO-7-NITROBENZOFURAZAN / INHIBITION | ||||||
Function / homology | ![]() Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase complex / 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 ...Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase complex / 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 / ADP binding / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Orriss, G.L. / Leslie, A.G.W. / Braig, K. / Walker, J.E. | ||||||
![]() | ![]() Title: Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. Authors: Orriss, G.L. / Leslie, A.G. / Braig, K. / Walker, J.E. #1: ![]() Title: Structure at 2.8 A Resolution of F1-ATPase from Bovine Heart Mitochondria Authors: Abrahams, J.P. / Leslie, A.G. / Lutter, R. / Walker, J.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 573.9 KB | Display | ![]() |
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PDB format | ![]() | 465.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.9 MB | Display | ![]() |
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Full document | ![]() | 2 MB | Display | |
Data in XML | ![]() | 106.3 KB | Display | |
Data in CIF | ![]() | 142 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 4 types, 7 molecules ABCDFEG
#1: Protein | Mass: 55301.207 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 51532.613 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | | Mass: 51667.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Protein | | Mass: 30185.674 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Non-polymers , 5 types, 175 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-MG / #6: Chemical | ChemComp-ATP / #7: Chemical | ChemComp-ADP / | #8: Chemical | ChemComp-PO4 / | #9: Water | ChemComp-HOH / | |
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-Details
Compound details | THE F1-ATPASE MOLECULE HAS THREE COPIES OF THE NON-CATALYTIC ALPHA SUBUNIT AND THREE COPIES OF THE ...THE F1-ATPASE MOLECULE HAS THREE COPIES OF THE NON-CATALYTIC ALPHA SUBUNIT AND THREE COPIES OF THE CATALYTIC BETA SUBUNIT. IN THE PRIMARY REFERENCE, THE BETA SUBUNITS WERE LABELLED ACCORDING TO THE BOUND NUCLEOTIDE |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 50MM TRIS-HCL, PH7.5, 200MM SODIUM CHLORIDE, 20MM MAGNESIUM SULPHATE, 1MM EDTA, 0.002% (W/V) PHENYL METHYLSULPHONYL FLUORIDE, 0.02%(W/V) SODIUM AZIDE, 10.5% (W/V) PEG MME 5000, 250UM AMP-PNP AND 5UM ADP. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / pH: 7.2 / Method: microdialysis | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 12, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 3→20 Å / Num. obs: 70240 / % possible obs: 97.2 % / Redundancy: 2.5 % / Biso Wilson estimate: 54.48 Å2 / Rmerge(I) obs: 0.088 / Net I/σ(I): 10.1 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.304 / Mean I/σ(I) obs: 3.4 / % possible all: 98 |
Reflection shell | *PLUS % possible obs: 98 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: ALUMINUM FLUORIDE INHIBITED FORM OF BOVINE MITOCHONDRIAL F1-ATPASE Resolution: 3→6 Å / Isotropic thermal model: INDIVIDUAL / Cross valid method: FREE-R / σ(F): 2
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Displacement parameters | Biso mean: 52.67 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.12 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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