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- PDB-6myt: Avian mitochondrial complex II with Atpenin A5 bound, sidechain i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6myt | ||||||
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Title | Avian mitochondrial complex II with Atpenin A5 bound, sidechain in pocket | ||||||
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![]() | OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / Complex II / membrane protein / heme protein / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex | ||||||
Function / homology | ![]() Citric acid cycle (TCA cycle) / The tricarboxylic acid cycle / succinate metabolic process / succinate dehydrogenase activity / TIM22 mitochondrial import inner membrane insertion complex / : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / protein insertion into mitochondrial inner membrane ...Citric acid cycle (TCA cycle) / The tricarboxylic acid cycle / succinate metabolic process / succinate dehydrogenase activity / TIM22 mitochondrial import inner membrane insertion complex / : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / protein insertion into mitochondrial inner membrane / oxidoreductase activity, acting on the CH-CH group of donors / anaerobic respiration / 3 iron, 4 sulfur cluster binding / protein transmembrane transporter activity / ubiquinone binding / tricarboxylic acid cycle / aerobic respiration / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / electron transfer activity / heme binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Berry, E.A. / Huang, L.-S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Crystallographic investigation of the ubiquinone binding site of respiratory Complex II and its inhibitors. Authors: Huang, L.S. / Lummen, P. / Berry, E.A. #1: ![]() Title: 3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme. Authors: Huang, L.S. / Sun, G. / Cobessi, D. / Wang, A.C. / Shen, J.T. / Tung, E.Y. / Anderson, V.E. / Berry, E.A. #2: ![]() Title: Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the "oxaloacetate-inhibited" state. Authors: Huang, L.S. / Shen, J.T. / Wang, A.C. / Berry, E.A. #3: Journal: Acta Crystallogr. D Biol. Crystallogr. / Year: 2005 Title: Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 A. Authors: Huang, L.S. / Borders, T.M. / Shen, J.T. / Wang, C.J. / Berry, E.A. #4: ![]() Title: Crystal structure of mitochondrial respiratory membrane protein complex II. Authors: Sun, F. / Huo, X. / Zhai, Y. / Wang, A. / Xu, J. / Su, D. / Bartlam, M. / Rao, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 480 KB | Display | ![]() |
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PDB format | ![]() | 386.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 43.9 KB | Display | |
Data in CIF | ![]() | 59.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6myoC ![]() 6mypC ![]() 6myqC ![]() 6myrC ![]() 6mysC ![]() 6myuC ![]() 1yq3S S: Starting model for refinement C: citing same article ( |
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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
-Succinate dehydrogenase [ubiquinone] ... , 3 types, 3 molecules ABD
#1: Protein | Mass: 68256.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: F1NPJ4, UniProt: Q9YHT1*PLUS, succinate dehydrogenase |
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#2: Protein | Mass: 28685.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#4: Protein | Mass: 10971.604 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein , 1 types, 1 molecules C
#3: Protein | Mass: 15391.153 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: D0VWW3, UniProt: A0A3Q2U2Y6*PLUS, succinate dehydrogenase |
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-Non-polymers , 13 types, 270 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/OAA.gif)
![](data/chem/img/K.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/SF4.gif)
![](data/chem/img/F3S.gif)
![](data/chem/img/AT5.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/UMQ.gif)
![](data/chem/img/3PE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/OAA.gif)
![](data/chem/img/K.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/SF4.gif)
![](data/chem/img/F3S.gif)
![](data/chem/img/AT5.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/UMQ.gif)
![](data/chem/img/3PE.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-FAD / | ||||||||||||||||||
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#6: Chemical | ChemComp-OAA / | ||||||||||||||||||
#7: Chemical | ChemComp-K / | ||||||||||||||||||
#8: Chemical | ChemComp-UNL / Num. of mol.: 59 / Source method: obtained synthetically #9: Chemical | ChemComp-PEG / | #10: Chemical | ChemComp-FES / | #11: Chemical | ChemComp-SF4 / | #12: Chemical | ChemComp-F3S / | #13: Chemical | ChemComp-AT5 / | #14: Chemical | ChemComp-HEM / | #15: Chemical | ChemComp-UMQ / | #16: Chemical | ChemComp-3PE / | #17: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.46 Å3/Da / Density % sol: 64.43 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 47 g/L PEG3350, 30 mL/L PEG400, 23 mL/L isopropanol, 0.05 M HEPES sodium, 0.01 M Tris-HCl, 3.1 mM manganese chloride, 0.62 mM magnesium chloride, 1.5 mM sodium azide, 0.25 mM sodium EDTA, 10 ...Details: 47 g/L PEG3350, 30 mL/L PEG400, 23 mL/L isopropanol, 0.05 M HEPES sodium, 0.01 M Tris-HCl, 3.1 mM manganese chloride, 0.62 mM magnesium chloride, 1.5 mM sodium azide, 0.25 mM sodium EDTA, 10 g/L octyl beta-D-glucoside, undecyl-beta-D-maltoside, crystal was soaked with Atpenin A5 after crystallization |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 1, 2007 |
Radiation | Monochromator: liquid nitrogen-cooled dual crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.27→25.23 Å / Num. obs: 70243 / % possible obs: 87.6 % / Redundancy: 2.15 % / Biso Wilson estimate: 42.29 Å2 / Rmerge(I) obs: 0.145 / Net I/σ(I): 4.1 |
Reflection shell | Resolution: 2.27→2.34 Å / Redundancy: 1.53 % / Rmerge(I) obs: 0.557 / Mean I/σ(I) obs: 1.5 / % possible all: 67.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1YQ3 Resolution: 2.27→25.19 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 33.36 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 60.5814 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.27→25.19 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 20.4176 Å / Origin y: 18.5239 Å / Origin z: 110.1542 Å
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Refinement TLS group | Selection details: ALL |