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Open data
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Basic information
Entry | Database: PDB / ID: 1g5x | ||||||
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Title | The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I | ||||||
![]() | BETA-KETOACYL ACYL CARRIER PROTEIN SYNTHASE I | ||||||
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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 / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Zhang, Y.M. / Rao, M.S. / Heath, R.J. / Price, A.C. / Olson, A.J. / Rock, C.O. / White, S.W. | ||||||
![]() | ![]() Title: Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III. Authors: Zhang, Y.M. / Rao, M.S. / Heath, R.J. / Price, A.C. / Olson, A.J. / Rock, C.O. / White, S.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 298.6 KB | Display | ![]() |
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PDB format | ![]() | 243.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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 assembly is the dimer formed by chains A and B / The biological assembly is the dimer formed by chains C and D |
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Components
#1: Protein | Mass: 42656.203 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() References: UniProt: P0A953, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: 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: 52.07 % | ||||||||||||||||||||
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Crystal grow![]() | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: ammonium sulfate, PEG 400, tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||
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: MACSCIENCE / Detector: IMAGE PLATE / Date: Dec 13, 1999 / Details: osmic confocal mirrors |
Radiation | Monochromator: osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.45→19.9 Å / Num. all: 64781 / Num. obs: 64781 / % possible obs: 96.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 38.9 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 21.5 |
Reflection shell | Resolution: 2.45→2.49 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.247 / Mean I/σ(I) obs: 5.7 / Num. unique all: 3015 / % possible all: 95.3 |
Reflection | *PLUS |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: beta-ketoacyl acyl carrier protein synthase II Resolution: 2.45→19.9 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.45→19.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.45→2.56 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 19.9 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.199 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.319 / Rfactor Rwork: 0.267 |