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Open data
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Basic information
Entry | Database: PDB / ID: 1l0v | |||||||||
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Title | Quinol-Fumarate Reductase with Menaquinol Molecules | |||||||||
![]() | (Fumarate reductase ...) x 4 | |||||||||
![]() | OXIDOREDUCTASE / fumarate reductase / succinate dehydrogenase / complex II / quinol / membrane protein | |||||||||
Function / homology | ![]() : / succinate dehydrogenase activity / fermentation / fumarate metabolic process / succinate dehydrogenase / anaerobic electron transport chain / succinate dehydrogenase (quinone) activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / iron-sulfur cluster binding ...: / succinate dehydrogenase activity / fermentation / fumarate metabolic process / succinate dehydrogenase / anaerobic electron transport chain / succinate dehydrogenase (quinone) activity / anaerobic respiration / 3 iron, 4 sulfur cluster binding / iron-sulfur cluster binding / bacterial-type flagellum assembly / tricarboxylic acid cycle / FAD binding / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / DNA damage response / membrane / metal ion binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Iverson, T.M. / Luna-Chavez, C. / Croal, L.R. / Cecchini, G. / Rees, D.C. | |||||||||
![]() | ![]() Title: Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. Authors: Iverson, T.M. / Luna-Chavez, C. / Croal, L.R. / Cecchini, G. / Rees, D.C. #1: ![]() Title: Structure of the E. coli Fumarate Reductase Respiratory Complex Authors: Iverson, T.M. / Luna-Chavez, C. / Cecchini, G. / Rees, D.C. #2: ![]() Title: Overexpression, Purification, and Crystallization of the Membrane-Bound Fumarate Reductase from Eschericia coli Authors: Luna-Chavez, C. / Iverson, T.M. / Rees, D.C. / Cecchini, G. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 399.5 KB | Display | ![]() |
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PDB format | ![]() | 321.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 890 KB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 66.1 KB | Display | |
Data in CIF | ![]() | 91.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kf6C ![]() 1kfyC ![]() 1fum C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 |
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Unit cell |
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Details | heterotetramer: two complete heterotetramers are observed in each asymmetric unit |
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Components
-Fumarate reductase ... , 4 types, 8 molecules AMBNCODP
#1: Protein | Mass: 66057.555 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 27021.885 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Protein | Mass: 14898.773 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Protein | Mass: 13118.870 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 7 types, 18 molecules ![](data/chem/img/OAA.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/F3S.gif)
![](data/chem/img/SF4.gif)
![](data/chem/img/MQ7.gif)
![](data/chem/img/CE1.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/F3S.gif)
![](data/chem/img/SF4.gif)
![](data/chem/img/MQ7.gif)
![](data/chem/img/CE1.gif)
#5: Chemical | #6: Chemical | #7: Chemical | #8: Chemical | #9: Chemical | #10: Chemical | ChemComp-MQ7 / #11: Chemical | ChemComp-CE1 / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.79 Å3/Da / Density % sol: 67.53 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: PEG 10000, MgAcetate, NaCitrate, DTT, EDTA, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.8 | ||||||||||||||||||||||||||||||||||||||||||||||||
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: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 1, 1998 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.65 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→50 Å / Num. obs: 49332 / % possible obs: 87.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.4 % / Biso Wilson estimate: 75 Å2 / Rsym value: 0.093 / Net I/σ(I): 15.5 |
Reflection shell | Resolution: 3.3→3.42 Å / Mean I/σ(I) obs: 6.5 / Rsym value: 0.277 / % possible all: 90 |
Reflection | *PLUS Lowest resolution: 50 Å / Num. measured all: 219456 / Rmerge(I) obs: 0.093 |
Reflection shell | *PLUS % possible obs: 90 % / Rmerge(I) obs: 0.277 / Mean I/σ(I) obs: 6.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FUM ![]() 1fum Resolution: 3.3→50 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3.3→50 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 50 Å / σ(F): 0 / Rfactor obs: 0.245 / Rfactor Rfree: 0.29 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS Type: c_bond_d / Dev ideal: 0.014 |