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- PDB-6hg8: Crystal structure of the R460G disease-causing mutant of the huma... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6hg8 | |||||||||||||||||||||||||||
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Title | Crystal structure of the R460G disease-causing mutant of the human dihydrolipoamide dehydrogenase. | |||||||||||||||||||||||||||
![]() | Dihydrolipoyl dehydrogenase, mitochondrial | |||||||||||||||||||||||||||
![]() | OXIDOREDUCTASE / lipoamide dehydrogenase (E3) component / disease-causing mutant / E3 deficiency | |||||||||||||||||||||||||||
Function / homology | ![]() acetyltransferase complex / acrosomal matrix / Glycine degradation / : / dihydrolipoyl dehydrogenase / dihydrolipoyl dehydrogenase activity / acetyl-CoA biosynthetic process from pyruvate / Lysine catabolism / oxoglutarate dehydrogenase complex / : ...acetyltransferase complex / acrosomal matrix / Glycine degradation / : / dihydrolipoyl dehydrogenase / dihydrolipoyl dehydrogenase activity / acetyl-CoA biosynthetic process from pyruvate / Lysine catabolism / oxoglutarate dehydrogenase complex / : / branched-chain amino acid catabolic process / Citric acid cycle (TCA cycle) / pyruvate dehydrogenase complex / Branched-chain amino acid catabolism / Pyruvate metabolism / Glyoxylate metabolism and glycine degradation / Regulation of pyruvate dehydrogenase (PDH) complex / motile cilium / sperm capacitation / Signaling by Retinoic Acid / mitochondrial electron transport, NADH to ubiquinone / gastrulation / Mitochondrial protein degradation / regulation of membrane potential / flavin adenine dinucleotide binding / mitochondrial matrix / mitochondrion / proteolysis / nucleus Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||||||||||||||
![]() | Ambrus, A. / Szabo, E. / Weichsel, A. / Bui, D. / Wilk, P. / Torocsik, B. / Weiss, M.S. / Montfort, W.R. / Jordan, F. / Adam-Vizi, V. | |||||||||||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Crystal structure of the R460G disease-causing mutant of the human dihydrolipoamide dehydrogenase. Authors: Ambrus, A. / Szabo, E. / Weichsel, A. / Bui, D. / Torocsik, B. / Montfort, W.R. / Jordan, F. / Adam-Vizi, V. | |||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 221.8 KB | Display | ![]() |
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PDB format | ![]() | 171.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 975.5 KB | Display | ![]() |
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Full document | ![]() | 985.5 KB | Display | |
Data in XML | ![]() | 45.4 KB | Display | |
Data in CIF | ![]() | 68.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zmdS 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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Unit cell |
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Components
#1: Protein | Mass: 52537.027 Da / Num. of mol.: 2 / Mutation: R460G Source method: isolated from a genetically manipulated source Details: Crystallized in 2 M (NH4)2SO4, 2 v/v% PEG-400, 0.1 M HEPES (pH 6.9). Source: (gene. exp.) ![]() Details (production host): N-terminal Strep-tag (for affinity purification) Production host: ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-TRS / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.87 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 6.9 Details: protein in: 100 mM Tris,150 mM NaCl, 1 mM EDTA, pH 8.0 reservoir solution: 2 M (NH4)2SO4, 2 v/v% PEG-400, 0.1 M HEPES (pH 6.9) volume ratio: 1 Temp details: 20 oC incubator |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 26, 2017 |
Radiation | Monochromator: Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.76→48.4 Å / Num. obs: 114691 / % possible obs: 93 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.8 % / CC1/2: 0.998 / Rmerge(I) obs: 0.141 / Net I/σ(I): 9.5 |
Reflection shell | Resolution: 1.76→1.86 Å / Redundancy: 6.7 % / Rmerge(I) obs: 0.255 / Mean I/σ(I) obs: 0.59 / Num. unique obs: 14032 / CC1/2: 0.365 / % possible all: 71.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ZMD Resolution: 1.76→30 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.952 / SU B: 4.215 / SU ML: 0.118 / Cross valid method: THROUGHOUT / ESU R: 0.111 / ESU R Free: 0.118 / Details: HYDROGENS HAVE BEEN ADDED IN THE 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.417 Å2
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Refinement step | Cycle: 1 / Resolution: 1.76→30 Å
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Refine LS restraints |
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