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- PDB-8gbt: Time-resolve SFX structure of a photoproduct of carbon monoxide c... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8gbt | ||||||||||||
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Title | Time-resolve SFX structure of a photoproduct of carbon monoxide complex of bovine cytochrome c oxidase | ||||||||||||
![]() | (Cytochrome c oxidase subunit ...) x 13 | ||||||||||||
![]() | MEMBRANE PROTEIN / Oxidative phosphorylation / Electron transfer chain / Bioenergetics / Cytochrome c oxidase / Serial femtosecond X-ray crystallography | ||||||||||||
Function / homology | ![]() TP53 Regulates Metabolic Genes / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / mitochondrial respirasome assembly / respiratory chain complex IV / : / regulation of oxidative phosphorylation / Respiratory electron transport / cytochrome-c oxidase / : ...TP53 Regulates Metabolic Genes / Cytoprotection by HMOX1 / respiratory chain complex IV assembly / mitochondrial respirasome assembly / respiratory chain complex IV / : / regulation of oxidative phosphorylation / Respiratory electron transport / cytochrome-c oxidase / : / oxidative phosphorylation / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / Mitochondrial protein degradation / electron transport coupled proton transport / ATP synthesis coupled electron transport / enzyme regulator activity / central nervous system development / mitochondrial inner membrane / oxidoreductase activity / copper ion binding / heme binding / mitochondrion / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Ishigami, I. / Yeh, S.-R. / Rousseau, D.L. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Detection of a Geminate Photoproduct of Bovine Cytochrome c Oxidase by Time-Resolved Serial Femtosecond Crystallography. Authors: Ishigami, I. / Carbajo, S. / Zatsepin, N. / Hikita, M. / Conrad, C.E. / Nelson, G. / Coe, J. / Basu, S. / Grant, T. / Seaberg, M.H. / Sierra, R.G. / Hunter, M.S. / Fromme, P. / Fromme, R. / ...Authors: Ishigami, I. / Carbajo, S. / Zatsepin, N. / Hikita, M. / Conrad, C.E. / Nelson, G. / Coe, J. / Basu, S. / Grant, T. / Seaberg, M.H. / Sierra, R.G. / Hunter, M.S. / Fromme, P. / Fromme, R. / Rousseau, D.L. / Yeh, S.R. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 801.7 KB | Display | ![]() |
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PDB format | ![]() | 638.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 8.8 MB | Display | ![]() |
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Full document | ![]() | 9 MB | Display | |
Data in XML | ![]() | 154.1 KB | Display | |
Data in CIF | ![]() | 195 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Cytochrome c oxidase subunit ... , 13 types, 26 molecules ANBOCPDQERFSGTHUIVJWKXLYMZ
#1: Protein | Mass: 57093.852 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 26068.404 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | Mass: 29957.627 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Protein | Mass: 17179.646 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 12453.081 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #6: Protein | Mass: 10684.038 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #7: Protein | Mass: 9629.782 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #8: Protein | Mass: 10039.244 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #9: Protein | Mass: 8537.019 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #10: Protein | Mass: 6682.726 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #11: Protein | Mass: 6365.217 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #12: Protein/peptide | Mass: 5449.396 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #13: Protein/peptide | Mass: 4967.756 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Sugars , 1 types, 4 molecules ![](data/chem/img/DMU.gif)
#28: Sugar | ChemComp-DMU / |
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-Non-polymers , 16 types, 299 molecules ![](data/chem/img/HEA.gif)
![](data/chem/img/CU.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/TGL.gif)
![](data/chem/img/PGV.gif)
![](data/chem/img/CMO.gif)
![](data/chem/img/CUA.gif)
![](data/chem/img/CHD.gif)
![](data/chem/img/OH.gif)
![](data/chem/img/CDL.gif)
![](data/chem/img/PSC.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/PEK.gif)
![](data/chem/img/SAC.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CU.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/TGL.gif)
![](data/chem/img/PGV.gif)
![](data/chem/img/CMO.gif)
![](data/chem/img/CUA.gif)
![](data/chem/img/CHD.gif)
![](data/chem/img/OH.gif)
![](data/chem/img/CDL.gif)
![](data/chem/img/PSC.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/PEK.gif)
![](data/chem/img/SAC.gif)
![](data/chem/img/HOH.gif)
#14: Chemical | ChemComp-HEA / #15: Chemical | #16: Chemical | #17: Chemical | #18: Chemical | ChemComp-TGL / #19: Chemical | ChemComp-PGV / ( #20: Chemical | #21: Chemical | #22: Chemical | ChemComp-CHD / #23: Chemical | #24: Chemical | ChemComp-CDL / #25: Chemical | #26: Chemical | #27: Chemical | ChemComp-PEK / ( #29: Chemical | #30: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | Temperature: 277 K / Method: batch mode / pH: 6.8 / Details: PEG4000, Sodium Phosphate, decylmaltoside |
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-Data collection
Diffraction | Mean temperature: 293 K / Serial crystal experiment: Y |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: CS-PAD CXI-1 / Detector: PIXEL / Date: Jun 16, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.321 Å / Relative weight: 1 |
Reflection | Resolution: 1.759→32.45 Å / Num. obs: 172414 / % possible obs: 100 % / Redundancy: 6.9 % / CC1/2: 0.859 / Net I/σ(I): 6.92 |
Reflection shell | Resolution: 2.87→2.99 Å / Num. unique obs: 17697 / CC1/2: 0.226 / % possible all: 100 |
Serial crystallography sample delivery | Method: injection |
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Processing
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Refinement | Method to determine structure: ![]() Details: Hydrogens have been added in their riding positions
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.179 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→32.002 Å
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Refine LS restraints |
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LS refinement shell |
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