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- PDB-1grp: REGULATORY AND CATALYTIC MECHANISMS IN ESCHERICHIA COLI ISOCITRAT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1grp | ||||||
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Title | REGULATORY AND CATALYTIC MECHANISMS IN ESCHERICHIA COLI ISOCITRATE DEHYDROGENASE: MULTIPLE ROLES FOR N115 | ||||||
![]() | ISOCITRATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE (NAD(A)-CHOH(D)) / OXIDOREDUCTASE / NADP / PHOSPHORYLATION / GLYOXYLATE BYPASS | ||||||
Function / homology | ![]() isocitrate dehydrogenase (NADP+) / isocitrate dehydrogenase (NADP+) activity / glyoxylate cycle / guanosine tetraphosphate binding / tricarboxylic acid cycle / electron transport chain / NAD binding / response to oxidative stress / magnesium ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Grobler, J.A. / Hurley, J.H. | ||||||
![]() | ![]() Title: Second-site suppression of regulatory phosphorylation in Escherichia coli isocitrate dehydrogenase. Authors: Chen, R. / Grobler, J.A. / Hurley, J.H. / Dean, A.M. #1: ![]() Title: Regulation of Isocitrate Dehydrogenase by Phosphorylation Involves No Long-Range Conformational Change in the Free Enzyme Authors: Hurley, J.H. / Dean, A.M. / Thorsness, P.E. / Koshland Junior, D.E. / Stroud, R.M. #2: ![]() Title: Regulation of an Enzyme by Phosphorylation at the Active Site Authors: Hurley, J.H. / Dean, A.M. / Sohl, J.L. / Koshland Junior, D.E. / Stroud, R.M. #3: ![]() Title: Structure of a Bacterial Enzyme Regulated by Phosphorylation, Isocitrate Dehydrogenase Authors: Hurley, J.H. / Thorsness, P.E. / Ramalingam, V. / Helmers, N.H. / Koshland Junior, D.E. / Stroud, R.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.4 KB | Display | ![]() |
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PDB format | ![]() | 69.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 386.8 KB | Display | ![]() |
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Full document | ![]() | 395.4 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Data in CIF | ![]() | 14.7 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: CIS PROLINE - PRO 262 |
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Components
#1: Protein | Mass: 45794.594 Da / Num. of mol.: 1 / Mutation: N115L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P08200, isocitrate dehydrogenase (NADP+) |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ICT / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.54 Å3/Da / Density % sol: 72.9 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.4 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→100 Å / Num. obs: 28004 / % possible obs: 92.5 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.118 |
Reflection | *PLUS Rmerge(I) obs: 0.118 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.59 Å / % possible obs: 66.1 % / Num. unique obs: 1957 / Rmerge(I) obs: 0.298 / Mean I/σ(I) obs: 4.9 |
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Processing
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Refinement | Resolution: 2.5→6 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.5→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.199 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |