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Open data
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Basic information
Entry | Database: PDB / ID: 1kb9 | ||||||
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Title | YEAST CYTOCHROME BC1 COMPLEX | ||||||
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![]() | OXIDOREDUCTASE/ELECTRON TRANSPORT / ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / mitochondrial respiratory chain complex III assembly / Respiratory electron transport / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lange, C. / Nett, J.H. / Trumpower, B.L. / Hunte, C. | ||||||
![]() | ![]() Title: SPECIFIC ROLES OF PROTEIN-PHOSPHOLIPID INTERACTIONS IN THE YEAST CYTOCHROME BC1 COMPLEX STRUCTURE Authors: Lange, C. / Nett, J.H. / Trumpower, B.L. / Hunte, C. #1: ![]() Title: Structure Of The Yeast Cytochrome Bc1 Complex Co-Crystallized With An Antibody Fv-Fragment Authors: Hunte, C. / Koepke, J. / Lange, C. / Rossmanith, T. / Michel, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 461.3 KB | Display | ![]() |
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PDB format | ![]() | 377.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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
-UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX ... , 6 types, 6 molecules ABFGHI
#1: Protein | Mass: 47445.242 Da / Num. of mol.: 1 / Fragment: RESIDUES 27-457 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
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#2: Protein | Mass: 38751.918 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-368 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
#6: Protein | Mass: 8854.792 Da / Num. of mol.: 1 / Fragment: RESIDUES 74-147 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
#7: Protein | Mass: 14355.443 Da / Num. of mol.: 1 / Fragment: RESIDUES 3-127 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
#8: Protein | Mass: 10856.314 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-94 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
#9: Protein | Mass: 6301.232 Da / Num. of mol.: 1 / Fragment: RESIDUES 4-58 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
-Protein , 3 types, 3 molecules CDE
#3: Protein | ![]() Mass: 43674.535 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
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#4: Protein | ![]() Mass: 27521.020 Da / Num. of mol.: 1 / Fragment: RESIDUES 62-307 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
#5: Protein | Mass: 20122.955 Da / Num. of mol.: 1 / Fragment: RESIDUES 31-215 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Organelle: MITOCHONDRIA ![]() |
-Antibody , 2 types, 2 molecules JK
#10: Antibody | Mass: 14365.817 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#11: Antibody | Mass: 11926.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
-Non-polymers , 10 types, 333 molecules ![](data/chem/img/PCF.gif)
![](data/chem/img/UMQ.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/SMA.gif)
![](data/chem/img/UQ6.gif)
![](data/chem/img/PIE.gif)
![](data/chem/img/PEF.gif)
![](data/chem/img/CDL.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/UMQ.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/SMA.gif)
![](data/chem/img/UQ6.gif)
![](data/chem/img/PIE.gif)
![](data/chem/img/PEF.gif)
![](data/chem/img/CDL.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/HOH.gif)
#12: Chemical | ChemComp-PCF / ![]() | ||||||||||||||
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#13: Chemical | ChemComp-UMQ / | ||||||||||||||
#14: Chemical | ![]() #15: Chemical | ChemComp-SMA / | #16: Chemical | ChemComp-UQ6 / | #17: Chemical | ChemComp-PIE / | #18: Chemical | ![]() #19: Chemical | ChemComp-CDL / | ![]() #20: Chemical | ChemComp-FES / | ![]() #21: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.7 Å3/Da / Density % sol: 73.83 % |
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Crystal grow![]() | Method: vapor diffusion, sitting drop / pH: 8 / Details: PEG4000, pH 8, VAPOR DIFFUSION, SITTING DROP |
Crystal grow | *PLUS Method: unknown / Details: Hunte, C., (2000) Structure, 8, 669. |
-Data collection
Detector | Type: MARRESEARCH / Detector: CCD |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.3→14.96 Å / Num. all: 168517 / Num. obs: 168517 / Observed criterion σ(F): 0 / Biso Wilson estimate: 31.9 Å2 / Limit h max: 82 / Limit h min: -93 / Limit k max: 71 / Limit k min: -93 / Limit l max: 63 / Limit l min: 0 / Observed criterion F max: 3621196.32 / Observed criterion F min: 18.17 |
Reflection | *PLUS Highest resolution: 2.3 Å |
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Processing
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Refinement | Resolution: 2.3→14.96 Å / Rfactor Rfree error: 0.004 / Occupancy max: 1 / Occupancy min: 0 / Cross valid method: THROUGHOUT
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Solvent computation | Solvent model: CNS bulk solvent model used / Bsol: 38.6265 Å2 / ksol: 0.273859 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 157.38 Å2 / Biso mean: 69.92 Å2 / Biso min: 20.92 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→14.96 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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