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Yorodumi- PDB-1i12: CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1i12 | ||||||
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Title | CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA | ||||||
Components | GLUCOSAMINE-PHOSPHATE N-ACETYLTRANSFERASE | ||||||
Keywords | TRANSFERASE / GNAT / ALPHA/BETA | ||||||
Function / homology | Function and homology information Synthesis of UDP-N-acetyl-glucosamine / glucosamine-phosphate N-acetyltransferase / glucosamine 6-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine biosynthetic process / monosaccharide binding / endoplasmic reticulum-Golgi intermediate compartment / Golgi apparatus / endoplasmic reticulum / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.3 Å | ||||||
Authors | Peneff, C. / Mengin-Lecreulx, D. / Bourne, Y. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase. Authors: Peneff, C. / Mengin-Lecreulx, D. / Bourne, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i12.cif.gz | 153.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i12.ent.gz | 122.6 KB | Display | PDB format |
PDBx/mmJSON format | 1i12.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i1/1i12 ftp://data.pdbj.org/pub/pdb/validation_reports/i1/1i12 | HTTPS FTP |
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-Related 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 18259.021 Da / Num. of mol.: 4 / Mutation: S39C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: YFL017C / Plasmid: PQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15 (PREP4) References: UniProt: P43577, glucosamine-phosphate N-acetyltransferase #2: Chemical | ChemComp-ACO / #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: 2.44 Å3/Da / Density % sol: 43.7 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.1 Details: PEG 600, IMIDAZOLE, MALATE, pH 5.1, VAPOR DIFFUSION, HANGING DROP, temperature 20K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 | ||||||||||||||||||||||||||||||||||||||||||||||||
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: ESRF / Beamline: ID14-2 / Wavelength: 0.9326 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 16, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9326 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→26.82 Å / Num. all: 166110 / Num. obs: 547136 / % possible obs: 96.1 % / Observed criterion σ(I): 1.9 / Redundancy: 2.05 % / Biso Wilson estimate: 13.1 Å2 / Rsym value: 0.045 / Net I/σ(I): 7.9724 |
Reflection shell | Resolution: 1.3→1.35 Å / Redundancy: 1.8 % / Mean I/σ(I) obs: 1.9 / Num. unique all: 15590 / Rsym value: 0.376 / % possible all: 92.3 |
Reflection | *PLUS Lowest resolution: 30 Å / % possible obs: 96.6 % / Rmerge(I) obs: 0.045 |
Reflection shell | *PLUS % possible obs: 92.3 % / Rmerge(I) obs: 0.376 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.3→24.86 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 2235690.09 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 42.56 Å2 / ksol: 0.351 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.3→24.86 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.3→1.38 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 1.8 % / Rfactor obs: 0.21 / Rfactor Rwork: 0.21 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 18.1 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.299 / % reflection Rfree: 1.7 % / Rfactor Rwork: 0.288 |