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Yorodumi- PDB-3am5: K316A mutant of Enoyl-ACP Reductase from Plasmodium falciparum (P... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3am5 | ||||||
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Title | K316A mutant of Enoyl-ACP Reductase from Plasmodium falciparum (PfENR) in complex with triclosan | ||||||
Components | Enoyl-ACP reductaseEnoyl-acyl carrier protein reductase | ||||||
Keywords | OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / Triclosan / Enoyl-ACP reductase / mutant / oxidoreductase / P.falciparum / FabI / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex | ||||||
Function / homology | Function and homology information enoyl-[acyl-carrier-protein] reductase (NADH) activity / fatty acid biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | Plasmodium falciparum (malaria parasite P. falciparum) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.05 Å | ||||||
Authors | Maity, K. / Banerjee, T. / Narayanappa, P. / Surolia, N. / Surolia, A. / Suguna, K. | ||||||
Citation | Journal: Iubmb Life / Year: 2011 Title: Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from plasmodium falciparum Authors: Maity, K. / Banerjee, T. / Prabakaran, N. / Surolia, N. / Surolia, A. / Suguna, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3am5.cif.gz | 139.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3am5.ent.gz | 107.8 KB | Display | PDB format |
PDBx/mmJSON format | 3am5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/am/3am5 ftp://data.pdbj.org/pub/pdb/validation_reports/am/3am5 | HTTPS FTP |
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-Related structure data
Related structure data | 3am3C 3am4C 1uh5S S: Starting model for refinement C: citing same article (ref.) |
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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: 37186.086 Da / Num. of mol.: 2 / Fragment: residues 96-424 / Mutation: K316A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum) Gene: fabI / Plasmid: PET-28a(+)(NOVAGEN) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q9BJJ9, 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: 2.39 Å3/Da / Density % sol: 48.57 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 5.8 Details: 3M ammonium sulphate, 0.1M MES buffer, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Mar 18, 2009 / Details: Mirror |
Radiation | Monochromator: OSMIC MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→51.4 Å / Num. obs: 45800 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 9.8 % / Biso Wilson estimate: 26.6 Å2 / Rmerge(I) obs: 0.083 / Net I/σ(I): 20.3 |
Reflection shell | Resolution: 2.05→2.16 Å / Redundancy: 9.7 % / Rmerge(I) obs: 0.461 / Mean I/σ(I) obs: 4.4 / Num. unique all: 6576 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1UH5 Resolution: 2.05→47.85 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.943 / SU B: 3.554 / SU ML: 0.097 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.148 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: BULK SOLVENT MODEL USED
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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: 30.804 Å2
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Refinement step | Cycle: LAST / Resolution: 2.05→47.85 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.05→2.103 Å / Total num. of bins used: 20
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