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Yorodumi- PDB-1c14: CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX -
+Open data
-Basic information
Entry | Database: PDB / ID: 1c14 | ||||||
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Title | CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX | ||||||
Components | ENOYL REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / TRICLOSAN / FABI / ENOYL REDUCTASE | ||||||
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) / lipid biosynthetic process / enoyl-[acyl-carrier-protein] reductase (NADH) activity / 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) / lipid biosynthetic process / enoyl-[acyl-carrier-protein] reductase (NADH) activity / catalytic complex / protein homotetramerization / response to antibiotic / protein-containing complex / membrane / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2 Å | ||||||
Authors | Qiu, X. / Janson, C. / Court, R. / Smyth, M. / Payne, D. / Abdel-Meguid, S. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: Molecular basis for triclosan activity involves a flipping loop in the active site. Authors: Qiu, X. / Janson, C.A. / Court, R.I. / Smyth, M.G. / Payne, D.J. / Abdel-Meguid, S.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c14.cif.gz | 115 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c14.ent.gz | 88.8 KB | Display | PDB format |
PDBx/mmJSON format | 1c14.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c1/1c14 ftp://data.pdbj.org/pub/pdb/validation_reports/c1/1c14 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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: 53.65 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 300 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: (NH4)2SO4, PEG400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K | |||||||||||||||||||||||||
Crystal grow | *PLUS Details: drop consists of equal volume of protein and reservoir solutions | |||||||||||||||||||||||||
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 / Type: APS / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jan 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. all: 112233 / Num. obs: 21505 / % possible obs: 97 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.2 % / Biso Wilson estimate: 48 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 5 % / Rmerge(I) obs: 0.265 / % possible all: 93 |
Reflection | *PLUS Num. measured all: 112233 |
Reflection shell | *PLUS % possible obs: 93 % |
-Processing
Software |
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Refinement | Resolution: 2→7 Å / σ(F): 2 / σ(I): 2 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 2→7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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