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- PDB-1gc4: THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 CO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gc4 | ||||||
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Title | THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH ASPARTATE | ||||||
![]() | ASPARTATE AMINOTRANSFERASE![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ura, H. / Nakai, T. / Hirotsu, K. / Kuramitsu, S. | ||||||
![]() | ![]() Title: Substrate recognition mechanism of thermophilic dual-substrate enzyme. Authors: Ura, H. / Nakai, T. / Kawaguchi, S.I. / Miyahara, I. / Hirotsu, K. / Kuramitsu, S. #1: ![]() Title: Structure of Thermus thermuophilus HB8 Aspartate Aminotransferase and its Complex with Maleate Authors: Nakai, T. / Okada, K. / Akutsu, S. / Miyahara, I. / Kawaguchi, S. / Kato, R. / Kuramitsu, S. / Hirotsu, K. #2: ![]() Title: The Novel Substrate Recognition Mechanism Utilized by Aspartate Aminotransferse of the Extreme Thermophile Thermus thermophilus HB8 Authors: NOBE, Y. / Kawaguchi, S. / Ura, H. / Nakai, T. / Hirotsu, K. / Kato, R. / Kuramitsu, S. #3: ![]() Title: An Aspartate Aminotransferase from an Extremely Thermophilic Bacterium, Thermus thermophilus HB8 Authors: Okamoto, A. / Kato, R. / Masui, R. / Yamagishi, A. / Oshima, T. / Kuramitsu, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 297.6 KB | Display | ![]() |
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PDB format | ![]() | 240.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1b5oC ![]() 1b5pC ![]() 1gc3C ![]() 1gckC ![]() 5bj3C ![]() 5bj4C 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 42156.984 Da / Num. of mol.: 4 / Mutation: S14D, T16V, K101S, S261R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ASP / ![]() #3: Chemical | ChemComp-PLP / ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.25 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 6000, HEPES, sodium acetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jun 28, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.3→50 Å / Num. all: 32693 / Num. obs: 22781 / % possible obs: 97 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 1.6 % / Biso Wilson estimate: 45.3 Å2 / Rmerge(I) obs: 0.099 / Net I/σ(I): 3.9 |
Reflection shell | Resolution: 3.3→3.42 Å / Redundancy: 9.6 % / Rmerge(I) obs: 0.153 / Num. unique all: 2195 / % possible all: 94.7 |
Reflection | *PLUS Lowest resolution: 50 Å / Num. measured all: 274027 |
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Processing
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Refinement | Resolution: 3.3→8 Å / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3.3 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.217 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |