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Yorodumi- PDB-1hnj: CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + MALONYL-COA -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hnj | ||||||
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Title | CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + MALONYL-COA | ||||||
Components | BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III | ||||||
Keywords | TRANSFERASE / fabH | ||||||
Function / homology | Function and homology information beta-ketoacyl-[acyl-carrier-protein] synthase III / beta-ketoacyl-acyl-carrier-protein synthase III activity / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid metabolic process / fatty acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.46 Å | ||||||
Authors | Qiu, X. / Janson, C.A. / Smith, W.W. / Head, M. / Lonsdale, J. / Konstantinidis, A.K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Refined structures of beta-ketoacyl-acyl carrier protein synthase III. Authors: Qiu, X. / Janson, C.A. / Smith, W.W. / Head, M. / Lonsdale, J. / Konstantinidis, A.K. #1: Journal: J.Biol.Chem. / Year: 1999 Title: Crystal Structure of Beta-Ketoacyl-Acyl Carrier Protein Synthase III. A Key Condensing Enzyme in Bacterial Fatty Acid Biosynthesis Authors: Qiu, X. / Janson, C.A. / Konstantinidis, A.K. / Nwagwu, S. / Silverman, C. / Smith, W.W. / Khandekar, S.K. / Lonsdale, 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 | 1hnj.cif.gz | 77.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hnj.ent.gz | 57.7 KB | Display | PDB format |
PDBx/mmJSON format | 1hnj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hn/1hnj ftp://data.pdbj.org/pub/pdb/validation_reports/hn/1hnj | 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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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 33547.027 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: P0A6R0, beta-ketoacyl-[acyl-carrier-protein] synthase I |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-MLC / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.94 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.4 / Method: vapor diffusion / Details: Janson, C.A., (2000) Acta Crystallogr.D, 56, 747. | ||||||||||||||||||||||||||||||||||||||||||||||||
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: Jan 1, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.45→20 Å / Num. obs: 248087 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5 % / Rmerge(I) obs: 0.067 |
Reflection shell | Resolution: 1.45→1.5 Å / Redundancy: 5 % / Rmerge(I) obs: 0.275 / Num. unique all: 4742 / % possible all: 98.5 |
Reflection | *PLUS Num. obs: 49069 / Num. measured all: 248087 |
Reflection shell | *PLUS % possible obs: 98.5 % / Mean I/σ(I) obs: 3.2 |
-Processing
Software |
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Refinement | Resolution: 1.46→20 Å / σ(F): 0 / σ(I): 0 Details: No density for the malonyl-group and CP1-CP4 of Malonyl-CoA (MLC).
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Refinement step | Cycle: LAST / Resolution: 1.46→20 Å
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Refine LS restraints |
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