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- PDB-1ek4: BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH D... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ek4 | ||||||
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Title | BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH DODECANOIC ACID TO 1.85 RESOLUTION | ||||||
![]() | BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I | ||||||
![]() | TRANSFERASE / fatty acid synthase / thiolase fold / Claisen condensation / fatty acid substrate complex | ||||||
Function / homology | ![]() monounsaturated fatty acid biosynthetic process / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Olsen, J.G. / Kadziola, A. / Siggaard-Andersen, M. / von Wettstein-Knowles, P. / Larsen, S. | ||||||
![]() | ![]() Title: Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Authors: Olsen, J.G. / Kadziola, A. / von Wettstein-Knowles, P. / Siggaard-Andersen, M. / Larsen, S. #1: ![]() Title: The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I Authors: Olsen, J.G. / Kadziola, A. / von Wettstein-Knowles, P. / Siggaard-Andersen, M. / Lindquist, Y. / Larsen, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 309.8 KB | Display | ![]() |
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PDB format | ![]() | 260.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 400.7 KB | Display | ![]() |
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Full document | ![]() | 412.9 KB | Display | |
Data in XML | ![]() | 31.2 KB | Display | |
Data in CIF | ![]() | 50.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological entity is a dimer. There are two dimers in the asymmetric unit, one defined by chains A and B and one defined by chains C and D |
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Components
#1: Protein | Mass: 44073.707 Da / Num. of mol.: 4 Mutation: C163S, MRGSHHHHHHGS N-TERMINAL HIS-TAG (NOT IN MODEL) Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P0A953, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: Chemical | ChemComp-DAO / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.16 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 1.8 M ammonium sulfate, 2 % PEG400, 0.1 M bis-Tris propane, pH 6.5, resulting pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294K | |||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 260 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Nov 21, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→28.92 Å / Num. obs: 131071 / % possible obs: 85 % / Biso Wilson estimate: 10.1 Å2 / Rmerge(I) obs: 0.052 |
Reflection shell | Resolution: 1.85→1.97 Å / Rmerge(I) obs: 0.267 / Num. unique all: 15875 / % possible all: 65.1 |
Reflection | *PLUS % possible obs: 84 % / Rmerge(I) obs: 0.049 |
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Processing
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Refinement | Resolution: 1.85→28.92 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Eng & Huber
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Refinement step | Cycle: LAST / Resolution: 1.85→28.92 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||
Refine LS restraints | *PLUS
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