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- PDB-3lt1: Enoyl-ACP Reductase from Plasmodium falciparum (PfENR) in complex... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3lt1 | ||||||
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Title | Enoyl-ACP Reductase from Plasmodium falciparum (PfENR) in complex with triclosan variant T2 | ||||||
![]() | Enoyl-ACP reductase | ||||||
![]() | OXIDOREDUCTASE / Triclosan / Triclosan variant / Enoyl-ACP reductase / P.falciparum | ||||||
Function / homology | ![]() enoyl-[acyl-carrier-protein] reductase (NADH) activity / fatty acid biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Maity, K. / Bhargav, S.P. / Sankaran, B. / Surolia, N. / Surolia, A. / Suguna, K. | ||||||
![]() | ![]() Title: X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional ...Title: X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition Authors: Maity, K. / Bhargav, S.P. / Sankaran, B. / Surolia, N. / Surolia, A. / Suguna, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.8 KB | Display | ![]() |
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PDB format | ![]() | 105.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3lsyC ![]() 3lt0C ![]() 3lt2C ![]() 3lt4C ![]() 1uh5S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 37244.184 Da / Num. of mol.: 2 / Fragment: residues 96-424 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: fabI / Plasmid: PET-28a(+)(NOVAGEN) / Production host: ![]() ![]() 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: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.61 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 2.8-3M ammonium sulphate, 0.1M MES buffer, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 20, 2008 / Details: Vertically focusing RhPt coated mirror |
Radiation | Monochromator: Horizontally focussing asymmetric-cut single bounce Si(220) bent crystal monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9774 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→47.9 Å / Num. obs: 37309 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 10.6 % / Biso Wilson estimate: 34.5 Å2 / Rmerge(I) obs: 0.084 / Net I/σ(I): 24.3 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 8.3 % / Rmerge(I) obs: 0.729 / Mean I/σ(I) obs: 2.7 / Num. unique all: 3656 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1UH5 Resolution: 2.2→47.89 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.936 / SU B: 5.388 / SU ML: 0.134 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.228 / ESU R Free: 0.188 / 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: 35.809 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→47.89 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.199→2.256 Å / Total num. of bins used: 20
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