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Yorodumi- PDB-2fhs: Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reduct... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fhs | ||||||
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Title | Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli | ||||||
Components |
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Keywords | OXIDOREDUCTASE/BIOSYNTHETIC PROTEIN / PROTEIN-PROTEIN COMPLEX / OXIDOREDUCTASE-BIOSYNTHETIC PROTEIN COMPLEX | ||||||
Function / homology | Function and homology information enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) / NADH binding / biotin biosynthetic process / fatty acid elongation / enoyl-[acyl-carrier-protein] reductase (NADH) / acyl binding / enoyl-[acyl-carrier-protein] reductase (NADH) activity / lipid A biosynthetic process / lipid biosynthetic process / acyl carrier activity ...enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) / NADH binding / biotin biosynthetic process / fatty acid elongation / enoyl-[acyl-carrier-protein] reductase (NADH) / acyl binding / enoyl-[acyl-carrier-protein] reductase (NADH) activity / lipid A biosynthetic process / lipid biosynthetic process / acyl carrier activity / phosphopantetheine binding / catalytic complex / fatty acid biosynthetic process / protein homotetramerization / response to xenobiotic stimulus / response to antibiotic / lipid binding / protein-containing complex / membrane / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Kolappan, S. / Novichenok, P. / Rafi, S. / Simmerling, C. / Tonge, P.J. / Kisker, C. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: Structure of Acyl Carrier Protein Bound to FabI, the FASII Enoyl Reductase from Escherichia coli. Authors: Rafi, S. / Novichenok, P. / Kolappan, S. / Zhang, X. / Stratton, C.F. / Rawat, R. / Kisker, C. / Simmerling, C. / Tonge, P.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fhs.cif.gz | 111.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fhs.ent.gz | 86.2 KB | Display | PDB format |
PDBx/mmJSON format | 2fhs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fh/2fhs ftp://data.pdbj.org/pub/pdb/validation_reports/fh/2fhs | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-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 second part of the biological assembly is generated by: Y-X,Y,1/2-Z |
-Components
#1: Protein | Mass: 27892.926 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: str. K12 substr. W3110 / Production host: Escherichia coli (E. coli) References: GenBank: 85674894, UniProt: P0AEK4*PLUS, enoyl-[acyl-carrier-protein] reductase (NADH) #2: Protein | | Mass: 8645.460 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: acpP / Production host: Escherichia coli (E. coli) / References: UniProt: P0A6A8 #3: 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: 3.68 Å3/Da / Density % sol: 66.6 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 22% PEG 4000 and 1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 0.9783 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 22, 2003 |
Radiation | Monochromator: channel-cut Si(111) crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9783 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. all: 28138 / Num. obs: 27311 / % possible obs: 97.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.7→2.8 Å / % possible all: 98.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→30 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.91 / SU B: 21.284 / SU ML: 0.215 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.398 / ESU R Free: 0.287 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.385 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.77 Å / Total num. of bins used: 20
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