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- PDB-1xac: CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xac | ||||||
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Title | CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE. | ||||||
![]() | 3-ISOPROPYLMALATE DEHYDROGENASE 2T2M6T S82R | ||||||
![]() | OXIDOREDUCTASE / CHIMERA | ||||||
Function / homology | ![]() 3-isopropylmalate dehydrogenase / 3-isopropylmalate dehydrogenase activity / L-leucine biosynthetic process / amino acid biosynthetic process / NAD binding / magnesium ion binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Nagata, C. / Moriyama, H. / Tanaka, N. | ||||||
![]() | ![]() Title: Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme. Authors: Nagata, C. / Moriyama, H. / Tanaka, N. / Nakasako, M. / Yamamoto, M. / Ueki, T. / Oshima, T. #1: ![]() Title: The Crystal Structure of Thermostable Mutant of Chimeric 3-Isopropylmalate Dehydrogenase Authors: Sakurai, M. / Moriyama, H. / Onodera, K. / Kadono, S. / Numata, K. / Hayashi, Y. / Kawaguchi, J. / Yamagishi, A. / Oshima, T. / Tanaka, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 102.5 KB | Display | ![]() |
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PDB format | ![]() | 79.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.3 KB | Display | ![]() |
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Full document | ![]() | 382.4 KB | Display | |
Data in XML | ![]() | 9.7 KB | Display | |
Data in CIF | ![]() | 15.4 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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Atom site foot note | 1: ASN 80 - PRO 81 OMEGA = 217.92 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: CIS PROLINE - PRO 143 |
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Components
#1: Protein | Mass: 37056.246 Da / Num. of mol.: 1 / Mutation: 2T2M6T S82R Source method: isolated from a genetically manipulated source Details: CHIMERA IPMDH BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL 20% T MIDDLE 20% M RESIDUAL 60% T ORIGINAL 2T2M6T HAD BEEN MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE. Source: (gene. exp.) ![]() ![]() References: UniProt: P00351, UniProt: Q5SIY4*PLUS, 3-isopropylmalate dehydrogenase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.65 Å3/Da / Density % sol: 66.34 % | ||||||||||||||||||||
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Crystal | *PLUS Density % sol: 67.3 % | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 100 K / pH: 7.5 / Method: microdialysis | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.542 |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Sep 9, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.542 Å / Relative weight: 1 |
Reflection | Num. obs: 22097 / % possible obs: 67.2 % / Observed criterion σ(I): 1 / Redundancy: 0.672 % / Rmerge(I) obs: 0.05 |
Reflection | *PLUS Highest resolution: 2.1 Å / Rmerge(I) obs: 0.05 |
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Processing
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Refinement | Resolution: 2.1→8 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 33.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 21701 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 3.51 |