+Open data
-Basic information
Entry | Database: PDB / ID: 1i2z | ||||||
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Title | E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND BRL-12654 | ||||||
Components | ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] | ||||||
Keywords | OXIDOREDUCTASE / enoyl reductase / NAD / antibiotic | ||||||
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 / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.8 Å | ||||||
Authors | Heerding, D.A. / Miller, W.H. / Payne, D.J. / Janson, C.A. / Qiu, X. | ||||||
Citation | Journal: Bioorg.Med.Chem.Lett. / Year: 2001 Title: 1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI). Authors: Heerding, D.A. / Chan, G. / DeWolf, W.E. / Fosberry, A.P. / Janson, C.A. / Jaworski, D.D. / McManus, E. / Miller, W.H. / Moore, T.D. / Payne, D.J. / Qiu, X. / Rittenhouse, S.F. / Slater- ...Authors: Heerding, D.A. / Chan, G. / DeWolf, W.E. / Fosberry, A.P. / Janson, C.A. / Jaworski, D.D. / McManus, E. / Miller, W.H. / Moore, T.D. / Payne, D.J. / Qiu, X. / Rittenhouse, S.F. / Slater-Radosti, C. / Smith, W. / Takata, D.T. / Vaidya, K.S. / Yuan, C.C. / Huffman, W.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i2z.cif.gz | 112.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i2z.ent.gz | 87.2 KB | Display | PDB format |
PDBx/mmJSON format | 1i2z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1i2z_validation.pdf.gz | 638.8 KB | Display | wwPDB validaton report |
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Full document | 1i2z_full_validation.pdf.gz | 654.8 KB | Display | |
Data in XML | 1i2z_validation.xml.gz | 14.5 KB | Display | |
Data in CIF | 1i2z_validation.cif.gz | 20.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i2/1i2z ftp://data.pdbj.org/pub/pdb/validation_reports/i2/1i2z | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 27892.926 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: P29132, UniProt: P0AEK4*PLUS, 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: 2.65 Å3/Da / Density % sol: 53.56 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop / Details: Qiu, X., (1999) Protein Sci., 8, 2529. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. obs: 106190 / % possible obs: 96 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 7 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.8→2.85 Å / Redundancy: 7 % / Rmerge(I) obs: 0.117 / % possible all: 82 |
Reflection | *PLUS Lowest resolution: 20 Å / % possible obs: 96 % |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 2.8→7 Å / σ(F): 2 / σ(I): 2
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Refinement step | Cycle: LAST / Resolution: 2.8→7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 7 Å / σ(F): 2 / % reflection Rfree: 5 % | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
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