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- PDB-2ied: CRYSTAL STRUCTURE of ISONIAZID-RESISTANT S94A ENOYL-ACP(COA) REDU... -
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Basic information
Entry | Database: PDB / ID: 2ied | ||||||
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Title | CRYSTAL STRUCTURE of ISONIAZID-RESISTANT S94A ENOYL-ACP(COA) REDUCTASE MUTANT ENZYME FROM MYCOBACTERIUM TUBERCULOSIS UNCOMPLEXED | ||||||
![]() | Enoyl-[acyl-carrier-protein] reductase [NADH] | ||||||
![]() | OXIDOREDUCTASE / ENOYL-ACYL CARRIER PROTEIN / InhA reductase | ||||||
Function / homology | ![]() enoyl-[acyl-carrier-protein] reductase [NAD(P)H] activity / trans-2-enoyl-CoA reductase (NADH) activity / mycolic acid biosynthetic process / fatty acid elongation / enoyl-[acyl-carrier-protein] reductase (NADH) / enoyl-[acyl-carrier-protein] reductase (NADH) activity / NAD+ binding / peptidoglycan-based cell wall / fatty acid binding / fatty acid biosynthetic process ...enoyl-[acyl-carrier-protein] reductase [NAD(P)H] activity / trans-2-enoyl-CoA reductase (NADH) activity / mycolic acid biosynthetic process / fatty acid elongation / enoyl-[acyl-carrier-protein] reductase (NADH) / enoyl-[acyl-carrier-protein] reductase (NADH) activity / NAD+ binding / peptidoglycan-based cell wall / fatty acid binding / fatty acid biosynthetic process / response to antibiotic / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dias, M.V.B. / Prado, A.M.X. / Vasconcelos, I.B. / Fadel, V. / Basso, L.A. / Santos, D.S. / Azevedo Jr., W.F. | ||||||
![]() | ![]() Title: Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis. Authors: Dias, M.V. / Vasconcelos, I.B. / Prado, A.M. / Fadel, V. / Basso, L.A. / de Azevedo, W.F. / Santos, D.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 219.7 KB | Display | ![]() |
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PDB format | ![]() | 176 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464.1 KB | Display | ![]() |
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Full document | ![]() | 527 KB | Display | |
Data in XML | ![]() | 54.7 KB | Display | |
Data in CIF | ![]() | 77.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2idzC ![]() 2ie0C ![]() 2iebC ![]() 1p44S C: citing same article ( 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: 28407.586 Da / Num. of mol.: 4 / Mutation: S94A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A5Y6, UniProt: P9WGR1*PLUS, enoyl-[acyl-carrier-protein] reductase (NADH) #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 36.08 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 100 mM sodium citrate, pH 5.6, 200 mM ammonium acetate and 20-30% of the PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 130 mm / Detector: CCD / Date: Mar 22, 2006 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.427 Å / Relative weight: 1 |
Reflection | Resolution: 2.14→45.41 Å / Num. all: 44679 / Num. obs: 44054 / % possible obs: 98.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.058 |
Reflection shell | Resolution: 2.14→2.26 Å / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 2 / Num. unique all: 5868 / % possible all: 85.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1P44 Resolution: 2.14→42.26 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.894 / SU B: 6.398 / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / ESU R: 0.397 / ESU R Free: 0.258 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 28.459 Å2
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Refinement step | Cycle: LAST / Resolution: 2.14→42.26 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.14→2.198 Å / Total num. of bins used: 20
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