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Open data
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Basic information
Entry | Database: PDB / ID: 2iwy | ||||||
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Title | Human mitochondrial beta-ketoacyl ACP synthase | ||||||
![]() | 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE | ||||||
![]() | TRANSFERASE / MITOCHONDRIA / MITOCHONDRION / LIPID SYNTHESIS / FATTY ACID SYNTHESIS / FATTY ACID BIOSYNTHESIS / BETA-KETOACYL ACP SYNTHASE / TRANSIT PEPTIDE / ACYLTRANSFERASE / CLAISEN CONDENSATION / KAS / CERULENIN / HOMO SAPIENS | ||||||
Function / homology | ![]() short-chain fatty acid biosynthetic process / medium-chain fatty acid biosynthetic process / acyl-CoA metabolic process / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] synthase activity / Mitochondrial protein degradation / fatty acid biosynthetic process / mitochondrial matrix / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Christensen, C.E. / Kragelund, B.B. / von Wettstein-Knowles, P. / Henriksen, A. | ||||||
![]() | ![]() Title: Structure of the Human Beta-Ketoacyl [Acp] Synthase from the Mitochondrial Type II Fatty Acid Synthase. Authors: Christensen, C.E. / Kragelund, B.B. / von Wettstein-Knowles, P. / Henriksen, A. #1: Journal: J.Biol.Chem. / Year: 2005 Title: Cloning, Expression, and Characterization of the Human Mitochondrial Beta-Ketoacyl Synthase Authors: Zhang, L. / Joshi, A.K. / Hofmann, J. / Schweizer, E. / Smith, S. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 175.5 KB | Display | ![]() |
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PDB format | ![]() | 138.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 444.4 KB | Display | ![]() |
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Full document | ![]() | 447.7 KB | Display | |
Data in XML | ![]() | 33.3 KB | Display | |
Data in CIF | ![]() | 48.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2iwzC ![]() 2ix4C ![]() 1w0iS C: citing same article ( 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: 46439.566 Da / Num. of mol.: 2 / Fragment: RESIDUES 38-459 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9NWU1, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | GENETICALL | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.8 % |
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Crystal grow | pH: 7.8 / Details: 24% PEG-3350, 0.2 M NH4CL, pH 7.80 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 4, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.063 Å / Relative weight: 1 |
Reflection | Resolution: 2→36.9 Å / Num. obs: 51373 / % possible obs: 98.1 % / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 22.73 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.8 |
Reflection shell | Resolution: 2→2.15 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 2.7 / % possible all: 96.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1W0I Resolution: 2.06→36.94 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.941 / SU B: 7.59 / SU ML: 0.106 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.191 / ESU R Free: 0.161 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: DISORDERED SIDE CHAINS ARE NOT INCLUDE IN THE THE MODEL.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.73 Å2
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Refinement step | Cycle: LAST / Resolution: 2.06→36.94 Å
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Refine LS restraints |
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