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- PDB-1gex: CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gex | ||||||
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Title | CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH HISTIDINOL-PHOSPHATE | ||||||
![]() | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE / alpha/beta-structure / Aminotransferase / PYRIDOXAL-5'-PHOSPHATE / PHOSPHORIC ACID MONO-[2-AMINO-3-(3H-IMIDAZOL-4-YL)-PROPYL]ESTER / 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 | ![]() | 60.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 399 KB | Display | ![]() |
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Full document | ![]() | 402.8 KB | Display | |
Data in XML | ![]() | 9.1 KB | Display | |
Data in CIF | ![]() | 13.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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-PLP / |
#3: Chemical | ChemComp-HSA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.19 % | ||||||||||||||||||||||||||||||||||||
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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 | ||||||||||||||||||||||||||||||||||||
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: Dec 25, 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: 2.2→50 Å / Num. all: 18942 / Num. obs: 18942 / % possible obs: 98.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 27.4 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.231 / Num. unique all: 1811 / % possible all: 95.5 |
Reflection | *PLUS Num. measured all: 87507 |
Reflection shell | *PLUS % possible obs: 95.5 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.335 / Rfactor Rwork: 0.285 |