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- PDB-6fn6: Modifying region (DH-ER-KR) of an insect fatty acid synthase (FAS) -
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Open data
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Basic information
Entry | Database: PDB / ID: 6fn6 | ||||||
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Title | Modifying region (DH-ER-KR) of an insect fatty acid synthase (FAS) | ||||||
![]() | Fatty acid synthase 1, isoform A | ||||||
![]() | TRANSFERASE / Dehydratase / Enoylreductase / Ketoreductase / lipid metabolism / fatty acid | ||||||
Function / homology | ![]() : / : / : / triglyceride biosynthetic process / : / : / : / cellular response to sucrose stimulus / : / : ...: / : / : / triglyceride biosynthetic process / : / : / : / cellular response to sucrose stimulus / : / : / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / : / [acyl-carrier-protein] S-acetyltransferase activity / oleoyl-[acyl-carrier-protein] hydrolase / : / response to sucrose / [acyl-carrier-protein] S-malonyltransferase activity / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / fatty acid synthase activity / glycogen metabolic process / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Benning, F.M.C. / Bukhari, H.S.T. / Jakob, R.P. / Maier, T. | ||||||
![]() | ![]() Title: Modifying region (DH-ER-KR) of an insect fatty acid synthase (FAS) Authors: Benning, F.M.C. / Bukhari, H.S.T. / Jakob, R.P. / Maier, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2vz9S 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: 129504.859 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: FASN1, anon-EST:Posey235, anon-EST:Posey43, anon-WO0138581.1, BcDNA:GH07626, BcDNA:gh07626, dFAS, DM_7295848, Dmel\CG3523, FAS, Fas, fas, FAS[CG3523], FASN, FASN[CG3523], Fatty acid synthase, CG3523, Dmel_CG3523 Plasmid: pAB1G Details (production host): Gateway-compatible pACEBAC plasmid Cell line (production host): 21 / Production host: ![]() ![]() References: UniProt: Q9VQL7, 3-oxoacyl-[acyl-carrier-protein] reductase, EC: 1.3.1.10, [acyl-carrier-protein] S-acetyltransferase, [acyl-carrier-protein] S-malonyltransferase, beta-ketoacyl-[acyl- ...References: UniProt: Q9VQL7, 3-oxoacyl-[acyl-carrier-protein] reductase, EC: 1.3.1.10, [acyl-carrier-protein] S-acetyltransferase, [acyl-carrier-protein] S-malonyltransferase, beta-ketoacyl-[acyl-carrier-protein] synthase I, fatty-acid synthase system, oleoyl-[acyl-carrier-protein] hydrolase, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.12 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.1 M Bis-Tris propane pH 6.5, 0.35 M Na Br, 17.5% PEG 3350, 10 mM NADP+ |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Feb 8, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.00003 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→129.729 Å / Num. obs: 68241 / % possible obs: 96 % / Redundancy: 24.06 % / Biso Wilson estimate: 54.01 Å2 / CC1/2: 0.998 / Rrim(I) all: 0.24 / Net I/σ(I): 15.57 |
Reflection shell | Resolution: 2.7→2.797 Å / Redundancy: 20.87 % / Mean I/σ(I) obs: 2.33 / Num. unique obs: 6989 / CC1/2: 0.832 / Rrim(I) all: 1.81 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2vz9 Resolution: 2.7→129.729 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 27.1
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→129.729 Å
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Refine LS restraints |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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