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- PDB-1s5o: Structural and Mutational Characterization of L-carnitine Binding... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1s5o | ||||||
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Title | Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase | ||||||
![]() | carnitine acetyltransferase isoform 2 | ||||||
![]() | TRANSFERASE / Carnitine acetyltransferase / binary complex / steady-state enzyme kinetics / substrate binding site | ||||||
Function / homology | ![]() carnitine O-acetyltransferase / carnitine O-acetyltransferase activity / Beta-oxidation of pristanoyl-CoA / carnitine O-octanoyltransferase / acyl-CoA oxidase activity / carnitine O-octanoyltransferase activity / carnitine metabolic process, CoA-linked / fatty acid beta-oxidation using acyl-CoA oxidase / short-chain fatty acid metabolic process / medium-chain fatty acid metabolic process ...carnitine O-acetyltransferase / carnitine O-acetyltransferase activity / Beta-oxidation of pristanoyl-CoA / carnitine O-octanoyltransferase / acyl-CoA oxidase activity / carnitine O-octanoyltransferase activity / carnitine metabolic process, CoA-linked / fatty acid beta-oxidation using acyl-CoA oxidase / short-chain fatty acid metabolic process / medium-chain fatty acid metabolic process / peroxisomal matrix / Peroxisomal protein import / peroxisome / mitochondrial inner membrane / endoplasmic reticulum / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Govindasamy, L. / Kukar, T. / Lian, W. / Pedersen, B. / Gu, Y. / Agbandje-Mckenna, M. / Jin, S. / Mckenna, R. / Wu, D. | ||||||
![]() | ![]() Title: Structural and mutational characterization of l-carnitine binding to human carnitine acetyltransferase. Authors: Govindasamy, L. / Kukar, T. / Lian, W. / Pedersen, B. / Gu, Y. / Agbandje-McKenna, M. / Jin, S. / McKenna, R. / Wu, D. | ||||||
History |
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Remark 999 | SEQUENCE THE AUTHORS STATE THE ELECTRON DENSITY MAP CONFIRMS THE THR RESIDUE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 140.5 KB | Display | ![]() |
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PDB format | ![]() | 108.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 388.3 KB | Display | ![]() |
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Full document | ![]() | 403.7 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 24.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1nm8S 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: 69902.867 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-152 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.49 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: Bis-Tris, NaCl, PEG8000, L-Carnitine, hpCAT, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
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 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9504 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 58948 / % possible obs: 91.6 % / Observed criterion σ(F): 4 / Rsym value: 0.086 / Net I/σ(I): 4.12 |
Reflection shell | Resolution: 1.8→1.86 Å / Num. unique all: 5280 / Rsym value: 0.343 / % possible all: 83.3 |
Reflection | *PLUS Lowest resolution: 50 Å / Rmerge(I) obs: 0.086 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / % possible obs: 83.3 % / Rmerge(I) obs: 0.343 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1NM8 Resolution: 1.8→50 Å / σ(F): 4 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→50 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | ||||||||||||
Refinement | *PLUS Lowest resolution: 50 Å / σ(F): 5 / Rfactor Rfree: 0.223 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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