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- PDB-1gfz: FLAVOPIRIDOL INHIBITS GLYCOGEN PHOSPHORYLASE BY BINDING AT THE IN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gfz | ||||||
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Title | FLAVOPIRIDOL INHIBITS GLYCOGEN PHOSPHORYLASE BY BINDING AT THE INHIBITOR SITE | ||||||
![]() | GLYCOGEN PHOSPHORYLASE | ||||||
![]() | TRANSFERASE / GLYCOGEN PHOSPHORYLASE / GLYCOGEN METABOLISM / DIABETES / FLAVOPIRIDOL / INHIBITOR SITE | ||||||
Function / homology | ![]() glycogen phosphorylase / glycogen phosphorylase activity / linear malto-oligosaccharide phosphorylase activity / SHG alpha-glucan phosphorylase activity / glycogen catabolic process / skeletal muscle myofibril / pyridoxal phosphate binding / nucleotide binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Oikonomakos, N.G. / Zographos, S.E. / Skamnaki, V.T. / Tsitsanou, K.E. / Johnson, L.N. | ||||||
![]() | ![]() Title: Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site. Authors: Oikonomakos, N.G. / Schnier, J.B. / Zographos, S.E. / Skamnaki, V.T. / Tsitsanou, K.E. / Johnson, L.N. #1: ![]() Title: A New Allosteric Site in Glycogen Phosphorylase b as a Target for Drug Interactions Authors: Oikonomakos, N.G. / Skamnaki, V.T. / Tsitsanou, K.E. / Gavalas, N.G. / Johnson, L.N. #2: ![]() Title: Allosteric Inhibition of Glycogen Phosphorylase a by the Potential Antidiabetic Drug 3-Isopropyl 4-(2-Chlorophenyl)-1,4-Dihydro-1-Ethyl-2-Methyl-Pyridine-3,5,6-Tricarboxylate Authors: Oikonomakos, N.G. / Tsitsanou, K.E. / Zographos, S.E. / Skamnaki, V.T. / Goldmann, S. / Bischoff, 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 | ![]() | 180.5 KB | Display | ![]() |
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PDB format | ![]() | 142.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Components
#1: Protein | Mass: 97291.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-PLP / |
#3: Chemical | ChemComp-IMP / |
#4: Chemical | ChemComp-CFF / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.7 Details: A single native T-state GPb crystal was soaked in a solution containing 5 mM caffeine, 10 mM Bes, 0.1 mM EDTA buffer, pH 6.7 for 80 min, pH 6.70, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 IV / Detector: IMAGE PLATE / Date: Jun 27, 2000 |
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: 2.3→28.75 Å / Num. obs: 43063 / % possible obs: 98.3 % / Redundancy: 4.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 2.3→2.34 Å / Rmerge(I) obs: 0.412 / Mean I/σ(I) obs: 2.8 / % possible all: 94 |
Reflection | *PLUS Num. measured all: 310740 / Rmerge(I) obs: 0.1 |
Reflection shell | *PLUS % possible obs: 94 % |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2.3→28.75 Å / Cross valid method: R FREE / σ(F): 0 Details: the final model contains residues 13-256, 261-316, and 324-837. Residues where B-factor values of main chain atoms exceed 60^2 include 13-22, 209-211, 250-256, 313-316, 324-325, 550-557, and ...Details: the final model contains residues 13-256, 261-316, and 324-837. Residues where B-factor values of main chain atoms exceed 60^2 include 13-22, 209-211, 250-256, 313-316, 324-325, 550-557, and 831-837. Thes same regions are also poorly ordered in the native enzyme structure.
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Refinement step | Cycle: LAST / Resolution: 2.3→28.75 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||||
Refinement | *PLUS | |||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 33.8 Å2 | |||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.367 / Rfactor Rwork: 0.328 |