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Yorodumi- PDB-1mka: E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY IT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mka | ||||||
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Title | E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY ITS CLASSIC MECHANISM-BASED INACTIVATOR, 3-DECYNOYL-N-ACETYL CYSTEAMINE | ||||||
Components | BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE | ||||||
Keywords | FATTY ACID BIOSYNTHESIS | ||||||
Function / homology | Function and homology information trans-2-decenoyl-[acyl-carrier protein] isomerase / trans-2-decenoyl-acyl-carrier-protein isomerase activity / : / : / : / : / : / 3-hydroxyacyl-[acyl-carrier-protein] dehydratase / fatty acid biosynthetic process / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Leesong, M. | ||||||
Citation | Journal: Structure / Year: 1996 Title: Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Authors: Leesong, M. / Henderson, B.S. / Gillig, J.R. / Schwab, J.M. / Smith, J.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mka.cif.gz | 84.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mka.ent.gz | 63.1 KB | Display | PDB format |
PDBx/mmJSON format | 1mka.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mk/1mka ftp://data.pdbj.org/pub/pdb/validation_reports/mk/1mka | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.9125, 0.1902, -0.3623), Vector: |
-Components
#1: Protein | Mass: 18859.848 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: RA244 / Description: TAC PROMOTER / Gene: FABA / Plasmid: PRA244 / Gene (production host): FABA / Production host: Escherichia coli (E. coli) / References: UniProt: P0A6Q3, EC: 4.2.1.60 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47 % | ||||||||||||||||||||
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Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Mar 1, 1992 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 22030 / % possible obs: 95 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.048 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 26075 / % possible obs: 97 % |
-Processing
Software |
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Refinement | Resolution: 2→7 Å / σ(F): 1 Details: RESIDUES B 136 - B 137 FORM A POORLY ORDERED LOOP AND HAVE HIGH ISOTROPIC B-FACTORS.
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Displacement parameters | Biso mean: 19.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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