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- PDB-5kof: Crosslinked Crystal Structure of Type II Fatty Acid Synthase Keto... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5kof | ||||||
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Title | Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpP | ||||||
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![]() | TRANSFERASE / crosslinked / ketosynthase / ACP / complex | ||||||
Function / homology | ![]() monounsaturated fatty acid biosynthetic process / beta-ketoacyl-[acyl-carrier-protein] synthase I / lipid biosynthetic process / lipid A biosynthetic process / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / acyl binding / acyl carrier activity / fatty acid biosynthetic process / response to xenobiotic stimulus ...monounsaturated fatty acid biosynthetic process / beta-ketoacyl-[acyl-carrier-protein] synthase I / lipid biosynthetic process / lipid A biosynthetic process / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / acyl binding / acyl carrier activity / fatty acid biosynthetic process / response to xenobiotic stimulus / lipid binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Milligan, J.C. / Jackson, D.R. / Barajas, J.F. / Tsai, S.C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis for interactions between an acyl carrier protein and a ketosynthase. Authors: Milligan, J.C. / Lee, D.J. / Jackson, D.R. / Schaub, A.J. / Beld, J. / Barajas, J.F. / Hale, J.J. / Luo, R. / Burkart, M.D. / Tsai, S.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 192.5 KB | Display | ![]() |
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PDB format | ![]() | 151.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2vb9S 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: 42727.281 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() References: UniProt: P0A954, UniProt: P0A953*PLUS, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: Protein | Mass: 8645.460 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() References: UniProt: B7MJ81, UniProt: P0A6A8*PLUS #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.52 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.4 Details: 0.2 M Ammonium acetate, 0.1 M Sodium acetate pH 5.4, 20% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 31, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→48.978 Å / Num. obs: 37072 / % possible obs: 100 % / Redundancy: 2 % / CC1/2: 0.996 / Rmerge(I) obs: 0.04978 / Rsym value: 0.0704 / Net I/σ(I): 7.27 |
Reflection shell | Resolution: 2.4→2.486 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.3953 / Mean I/σ(I) obs: 1.76 / CC1/2: 0.824 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2VB9 Resolution: 2.4→48.978 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 27.13 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→48.978 Å
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Refine LS restraints |
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LS refinement shell |
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