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Yorodumi- PDB-1f91: BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I IN COMPLEX WITH C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f91 | ||||||
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Title | BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I IN COMPLEX WITH C10 FATTY ACID SUBSTRATE | ||||||
Components | BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I | ||||||
Keywords | TRANSFERASE / Thiolase fold family / Dimer | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Olsen, J.G. / Kadziola, A. / Wettstein-Knowles, P.V. / Siggaard-Andersen, M. / Larsen, S. | ||||||
Citation | Journal: Structure / Year: 2001 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f91.cif.gz | 299.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f91.ent.gz | 253.1 KB | Display | PDB format |
PDBx/mmJSON format | 1f91.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f9/1f91 ftp://data.pdbj.org/pub/pdb/validation_reports/f9/1f91 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 42668.191 Da / Num. of mol.: 4 / Mutation: C163S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: P0A953, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: Chemical | ChemComp-OH / #3: Chemical | ChemComp-DKA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.16 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 294 K / Method: vapor diffusion / pH: 7.4 Details: 1.9 M ammonium sulfate, 2% PEG400, 0.1 M bis-Tris propane pH 6.5, pH 7.4, VAPOR DIFFUSION, temperature 294K | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 263 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.5184 |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jun 10, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5184 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→500 Å / Num. all: 71413 / Num. obs: 70763 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 27.7 Å2 |
Reflection | *PLUS Rmerge(I) obs: 0.052 |
-Processing
Software |
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Refinement | Resolution: 2.4→500 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.4→500 Å
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.21 / Rfactor Rwork: 0.174 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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