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Yorodumi- PDB-1gew: CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gew | ||||||
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Title | CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE | ||||||
Components | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE | ||||||
Keywords | TRANSFERASE / alpha/beta-structure / Aminotransferase / PYRIDOXAL-5'-PHOSPHATE / complex | ||||||
Function / homology | Function and homology information histidinol-phosphate transaminase / histidinol-phosphate transaminase activity / L-histidine biosynthetic process / pyridoxal phosphate binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2 Å | ||||||
Authors | Haruyama, K. / Nakai, T. / Miyahara, I. / Hirotsu, K. / Mizuguchi, H. / Hayashi, H. / Kagamiyama, H. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Authors: Haruyama, K. / Nakai, T. / Miyahara, I. / Hirotsu, K. / Mizuguchi, H. / Hayashi, H. / Kagamiyama, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gew.cif.gz | 80.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gew.ent.gz | 59.9 KB | Display | PDB format |
PDBx/mmJSON format | 1gew.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ge/1gew ftp://data.pdbj.org/pub/pdb/validation_reports/ge/1gew | 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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Details | The biological assembly is a dimer constructed from chain A a symmetry partner generated by the two-fold. |
-Components
#1: Protein | Mass: 39393.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: HISC / Plasmid: PUC118 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 References: UniProt: P06986, histidinol-phosphate transaminase |
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#2: Chemical | ChemComp-PLP / |
#3: 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: 2.42 Å3/Da / Density % sol: 49.15 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.7 Details: PEG 4000, magnesium chloride, tris, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 18, 1999 |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. all: 25542 / Num. obs: 25542 / % possible obs: 96.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Biso Wilson estimate: 24 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 12.7 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 1.3 % / Rmerge(I) obs: 0.23 / Num. unique all: 2152 / % possible all: 85.6 |
Reflection | *PLUS Num. measured all: 88073 |
Reflection shell | *PLUS % possible obs: 85.6 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2→8 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | |||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.332 / Rfactor Rwork: 0.312 |