+Open data
-Basic information
Entry | Database: PDB / ID: 3pjf | ||||||
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Title | Structure of ENR G93V mutant-NAD+-triclosan complex | ||||||
Components | Enoyl-[acyl-carrier-protein] reductase [NADH] | ||||||
Keywords | OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / ANTIBIOTIC RESISTANCE / FATTY ACID BIOSYNTHESIS / INNER MEMBRANE / LIPID SYNTHESIS / MEMBRANE / NAD / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR 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) / enoyl-[acyl-carrier-protein] reductase (NADH) activity / lipid biosynthetic process / catalytic complex / protein homotetramerization / response to antibiotic ...enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) / NADH binding / biotin biosynthetic process / fatty acid elongation / enoyl-[acyl-carrier-protein] reductase (NADH) / enoyl-[acyl-carrier-protein] reductase (NADH) activity / lipid biosynthetic process / catalytic complex / protein homotetramerization / response to antibiotic / protein-containing complex / membrane / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Kim, H.T. / Shin, D.G. / Chang, H.J. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2011 Title: Structural basis of triclosan resistance Authors: Jiten Singh, N. / Shin, D.G. / Lee, H.M. / Kim, H.T. / Chang, H.J. / Cho, J.M. / Kim, K.S. / Ro, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3pjf.cif.gz | 114.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3pjf.ent.gz | 87.7 KB | Display | PDB format |
PDBx/mmJSON format | 3pjf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pj/3pjf ftp://data.pdbj.org/pub/pdb/validation_reports/pj/3pjf | HTTPS FTP |
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-Related structure data
Related structure data | 3pjdC 3pjeC 1c14S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 29006.146 Da / Num. of mol.: 2 / Mutation: G93V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: ENVM, fabI / Plasmid: modified pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P0AEK4, enoyl-[acyl-carrier-protein] reductase (NADH) #2: Chemical | #3: Chemical | #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: 2.54 Å3/Da / Density % sol: 51.59 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.5M AMMONIUM CITRATE/AMMONIUM HYDROXIDE, 15% PEG8K, pH 8.50, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 4A / Wavelength: 1 / Wavelength: 1 Å | |||||||||
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Mar 11, 2007 | |||||||||
Radiation | Monochromator: SAGITALLY FOCUSED SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.9→50 Å / Num. obs: 46610 / % possible obs: 94.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 11.4 % / Biso Wilson estimate: 17 Å2 / Rmerge(I) obs: 0.083 / Rsym value: 0.076 | |||||||||
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.276 / Mean I/σ(I) obs: 4.43 / Num. unique all: 4310 / Rsym value: 0.306 / % possible all: 90.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1C14 Resolution: 1.9→50 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 50577.18 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 43.26 Å2 / ksol: 0.37 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→50 Å
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Refine LS restraints |
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LS refinement shell |
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Xplor file |
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