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- PDB-4icd: REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4icd | ||||||
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Title | REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME | ||||||
![]() | PHOSPHORYLATED ISOCITRATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE (NAD(A)-CHOH(D)) | ||||||
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 | ![]() | ||||||
![]() | Hurley, J.H. / Dean, A.M. / Thorsness, P.E. / Koshlandjunior, D.E. / Stroud, R.M. | ||||||
![]() | ![]() 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 Jr., D.E. / Stroud, R.M. #1: ![]() Title: Structure of a Bacterial Enzyme Regulated by Phosphorylation, Isocitrate Dehydrogenase Authors: Hurley, J.H. / Thorsness, P.E. / Ramalingam, V. / Helmers, N.H. / Koshlandjunior, 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. / Koshlandjunior, 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 | ![]() | 89.2 KB | Display | ![]() |
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PDB format | ![]() | 72.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.8 KB | Display | ![]() |
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Full document | ![]() | 380.2 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 16.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: RESIDUE SER 113 IS A PHOSPHORYLATED SERINE. / 2: PRO 262 IS A CIS PROLINE. |
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Components
#1: Protein | Mass: 45889.543 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P08200, isocitrate dehydrogenase (NADP+) |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.52 Å3/Da / Density % sol: 72.8 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.4 / Method: unknown / Details: took J. H. Hurley et al.,from original paper | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Num. obs: 21162 / Observed criterion σ(F): 1 / Num. measured all: 156365 / Rmerge F obs: 0.121 |
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Processing
Software | Name: ![]() | ||||||||||||
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Refinement | Rfactor Rwork: 0.169 / Highest resolution: 2.5 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refinement | *PLUS Highest resolution: 2.5 Å / Rfactor obs: 0.169 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |