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- PDB-2qn9: Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2qn9 | ||||||
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Title | Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea | ||||||
![]() | Glycogen phosphorylase, muscle form | ||||||
![]() | TRANSFERASE / glycogenolysis / type 2 diabetes / Allosteric enzyme / Carbohydrate metabolism / Glycogen metabolism / Glycosyltransferase / Nucleotide-binding / Phosphoprotein / Pyridoxal phosphate | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Chrysina, E.D. / Tiraidis, C. / Alexacou, K.-M. / Zographos, S.E. / Leonidas, D.D. / Oikonomakos, N.G. | ||||||
![]() | ![]() Title: N-(4-substituted-benzoyl)-N'-(beta-D-glucopyranosyl)ureas, inhibitors of glycogen phosphorylase: synthesis, kinetic and crystallographic evaluation Authors: Nagy, V. / Felf ldi, N. / Praly, J.-P. / Docsa, T. / Gergerly, P. / Chrysina, E.D. / Tiraidis, C. / Kosmopoulou, M.N. / Alexacou, K.-M. / Konstantakaki, 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 | ![]() | 184.1 KB | Display | ![]() |
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PDB format | ![]() | 143 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 521.4 KB | Display | ![]() |
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Full document | ![]() | 534.4 KB | Display | |
Data in XML | ![]() | 18.2 KB | Display | |
Data in CIF | ![]() | 29 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2qlmC ![]() 2qlnC ![]() 2qn3C ![]() 2qn7C ![]() 2qn8C ![]() 2qnbC ![]() 2prjS C: citing same article ( S: Starting model for refinement |
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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
#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: Sugar | ChemComp-NBX / |
#4: Chemical | ChemComp-IMP / |
#5: Water | ChemComp-HOH / |
Sequence details | AUTHORS STATE THAT RESIDUE 380 WAS AN ILE ACCORDING TO THE ELECTRON DENSITY. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.98 % |
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Crystal grow | Temperature: 289 K / Method: small tubes / pH: 6.7 Details: 10 mM Bes, 3 mM DDT, pH 6.7, SMALL TUBES, temperature 289K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Oct 31, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9076 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 65665 / Num. obs: 65665 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5.6 % / Biso Wilson estimate: 27.8 Å2 / Rsym value: 0.077 / Net I/σ(I): 16.2 |
Reflection shell | Resolution: 2→2.03 Å / Redundancy: 4.2 % / Mean I/σ(I) obs: 2.5 / Num. unique all: 3013 / Rsym value: 0.536 / % possible all: 92.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 2PRJ Resolution: 2→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.03 Å / Rfactor Rfree: 0.409 / Rfactor Rwork: 0.336 |