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- PDB-1e1y: 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: 1e1y | ||||||
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Title | Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site | ||||||
![]() | GLYCOGEN PHOSPHORYLASE, MUSCLE FORM | ||||||
![]() | TRANSFERASE / ALLOSTERIC INHIBITION | ||||||
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: 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. #2: ![]() Title: The Structure of Glycogen Phosphorylase B with an Alkyl-Dihydropyridine-Dicarboxylic Acid Compound, a Novel and Potent Inhibitor Authors: Zographos, S.E. / Oikonomakos, N.G. / Tsitsanou, K.E. / Leonidas, D.D. / Chrysina, E.D. / Skamnaki, V.T. / Bischoff, H. / Goldman, S. / Schramm, M. / Watson, K.A. / Johnson, L.N. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 192.8 KB | Display | ![]() |
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PDB format | ![]() | 151 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 511.1 KB | Display | ![]() |
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Full document | ![]() | 526.5 KB | Display | |
Data in XML | ![]() | 18.7 KB | Display | |
Data in CIF | ![]() | 31.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1c8kC ![]() 1gfzC ![]() 2gpaS S: Starting model for refinement 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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Unit cell |
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Components on special symmetry positions |
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Components
-Protein / Sugars , 2 types, 2 molecules A![](data/chem/img/GLC.gif)
![](data/chem/img/GLC.gif)
#1: Protein | Mass: 97291.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#4: Sugar | ChemComp-GLC / |
-Non-polymers , 4 types, 647 molecules ![](data/chem/img/CPB.gif)
![](data/chem/img/PO3.gif)
![](data/chem/img/PLP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PO3.gif)
![](data/chem/img/PLP.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CPB / |
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#3: Chemical | ChemComp-PO3 / |
#5: Chemical | ChemComp-PLP / |
#6: Water | ChemComp-HOH / |
-Details
Sequence details | 2AMV SWALL P00489 1 - 13 NOT IN ATOMS LI REFERENCE: K.NAKANO, P.K.HWANG, R.J.FLETTERICK, FEBS LETT. ...2AMV SWALL P00489 1 - 13 NOT IN ATOMS LI REFERENCE: K.NAKANO, P.K.HWANG, R.J.FLETTERICK |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.7 Details: AS DESCRIBED PREVIOUSLY BY OIKONOMAKOS ET AL. (1999) PROTEIN SCIENCE 8, 1930-1945., pH 6.70 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: co-crystallization | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Mar 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.05 Å / Relative weight: 1 |
Reflection | Resolution: 2.23→29.9 Å / Num. obs: 40691 / % possible obs: 87.3 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rmerge(I) obs: 0.104 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 2.23→2.27 Å / Rmerge(I) obs: 0.433 / Mean I/σ(I) obs: 2.4 / % possible all: 84.6 |
Reflection | *PLUS Num. measured all: 321450 |
Reflection shell | *PLUS % possible obs: 84.6 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2GPA Resolution: 2.23→29.9 Å / Cross valid method: FREE R-VALUE / σ(F): 0 Details: RESIDUES WHERE OVERALL -FACTOR VALUES EXCEED 60 A**2 INCLUDE 16-22 (71.1), 550-556 (69.4), AND 837-838 (75.9). TER PRO: RESIDUES 1-5,251-259,315-324,839- 842 WERE NOT DEFINED BY ELECTRON DENSITY
Refinement step | Cycle: LAST / Resolution: 2.23→29.9 Å |
Refine LS restraints |
Software | *PLUS Name: ![]() Refine LS restraints | *PLUS
LS refinement shell | *PLUS Rfactor Rfree: 0.314 / Rfactor Rwork: 0.252 |