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Yorodumi- PDB-1zow: Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protei... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zow | ||||||
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Title | Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III | ||||||
Components | 3-oxoacyl-[acyl-carrier-protein] synthase III | ||||||
Keywords | TRANSFERASE / FabH / fatty acid biosynthesis | ||||||
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 biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | Staphylococcus aureus subsp. aureus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Qiu, X. / Choudhry, A.E. / Janson, C.A. / Grooms, M. / Daines, R.A. / Lonsdale, J.T. / Khandekar, S.S. | ||||||
Citation | Journal: Protein Sci. / Year: 2005 Title: Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. Authors: Qiu, X. / Choudhry, A.E. / Janson, C.A. / Grooms, M. / Daines, R.A. / Lonsdale, J.T. / Khandekar, S.S. | ||||||
History |
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Remark 999 | SEQUENCE According to the author residues VAL60, GLU171 and LEU287 are correct based on the electron density. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zow.cif.gz | 254.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zow.ent.gz | 206.4 KB | Display | PDB format |
PDBx/mmJSON format | 1zow.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zo/1zow ftp://data.pdbj.org/pub/pdb/validation_reports/zo/1zow | HTTPS FTP |
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-Related structure data
Related structure data | 1hn9S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 33916.398 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus subsp. aureus (bacteria) Species: Staphylococcus aureus / Strain: MW2 / Production host: Escherichia coli (E. coli) References: UniProt: Q8NXE2, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: 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: 2.2 Å3/Da / Density % sol: 50 % |
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Crystal grow | Temperature: 273 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: PEG3K, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 273K |
-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: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 10, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 84128 / % possible obs: 96.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.085 |
Reflection shell | Resolution: 2→2.07 Å / Rmerge(I) obs: 0.231 / Mean I/σ(I) obs: 2.7 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1HN9 Resolution: 2→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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