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- PDB-1zid: LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zid | ||||||
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Title | LONG FATTY ACID CHAIN ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH AN ISONICOTINIC-ACYL-NADH INHIBITOR | ||||||
![]() | ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / INHA ENZYME / ISONIAZID / MODIFIED NADH / ENOYL-ACP REDUCTASE / TUBERCULOSIS / MYCOLIC ACID BIOSYNTHESIS / Structural Genomics / PSI / Protein Structure Initiative / TB Structural Genomics Consortium / TBSGC | ||||||
Function / homology | ![]() enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) / 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 activity (NAD(P)H) / 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 | ![]() | ||||||
![]() | Rozwarski, D.A. / Jacobs Jr., W.R. / Sacchettini, J.C. / TB Structural Genomics Consortium (TBSGC) | ||||||
![]() | ![]() Title: Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Authors: Rozwarski, D.A. / Grant, G.A. / Barton, D.H. / Jacobs Jr., W.R. / Sacchettini, J.C. #1: ![]() Title: Crystal Structure and Function of the Isoniazid Target of Mycobacterium Tuberculosis Authors: Dessen, A. / Quemard, A. / Blanchard, J.S. / Jacobs Junior, W.R. / Sacchettini, J.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.1 KB | Display | ![]() |
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PDB format | ![]() | 47.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 721.8 KB | Display | ![]() |
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Full document | ![]() | 731.7 KB | Display | |
Data in XML | ![]() | 14.2 KB | Display | |
Data in CIF | ![]() | 18.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1enyS S: Starting model for refinement |
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Similar structure data | |
Other databases |
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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: 28393.562 Da / Num. of mol.: 1 / Mutation: T2A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A5Y6, UniProt: P9WGR1*PLUS, enoyl-[acyl-carrier-protein] reductase (NADH) |
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#2: Chemical | ChemComp-ZID / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.58 Å3/Da / Density % sol: 65.6 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 12% MPD, 4% DMSO, 50MM NACITRATE, 100 MM HEPES, PH 7.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Nov 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: 0.005 MM NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→10 Å / Num. obs: 10621 / % possible obs: 90.7 % / Observed criterion σ(I): 1 / Rsym value: 0.164 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 2.7→2.77 Å / Mean I/σ(I) obs: 2.4 / Rsym value: 0.343 / % possible all: 49.5 |
Reflection | *PLUS Rmerge(I) obs: 0.164 |
Reflection shell | *PLUS % possible obs: 50 % / Rmerge(I) obs: 0.343 |
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Processing
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Refinement | Method to determine structure: INITIAL PHASES DERIVED FROM NATIVE STRUCTURE (PDB ENTRY 1ENY) Starting model: NATIVE STRUCTURE (PDB ENTRY 1ENY) Resolution: 2.7→10 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 24.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→10 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: 12
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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