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- PDB-1gey: CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gey | ||||||
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Title | CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE | ||||||
![]() | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE / alpha/beta-structure / N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE / PPE / complex | ||||||
Function / homology | ![]() histidinol-phosphate transaminase / histidinol-phosphate transaminase activity / L-histidine biosynthetic process / pyridoxal phosphate binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Haruyama, K. / Nakai, T. / Miyahara, I. / Hirotsu, K. / Mizuguchi, H. / Hayashi, H. / Kagamiyama, H. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 81.6 KB | Display | ![]() |
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PDB format | ![]() | 59.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446 KB | Display | ![]() |
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Full document | ![]() | 447.5 KB | Display | |
Data in XML | ![]() | 8.3 KB | Display | |
Data in CIF | ![]() | 12.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gewSC ![]() 1gexC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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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. |
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Components
#1: Protein | Mass: 39393.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P06986, histidinol-phosphate transaminase |
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#2: Chemical | ChemComp-PPE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.99 % | ||||||||||||||||||||||||||||||
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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: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Sep 26, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. all: 55982 / Num. obs: 55982 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Biso Wilson estimate: 30.225 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 10.17 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.265 / Num. unique all: 1628 / % possible all: 97.4 |
Reflection | *PLUS Num. obs: 16231 / Num. measured all: 55982 |
Reflection shell | *PLUS % possible obs: 97.4 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GEW Resolution: 2.3→8 Å / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.349 / Rfactor Rwork: 0.24 |