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- PDB-1ww2: Crystallographic studies on two bioisosteric analogues, N-acetyl-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ww2 | ||||||
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Title | Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase | ||||||
![]() | Glycogen phosphorylase, muscle form | ||||||
![]() | TRANSFERASE / glycogenolysis / type 2 diabetes | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Anagnostou, E. / Kosmopoulou, M.N. / Chrysina, E.D. / Leonidas, D.D. / Hadjiloi, T. / Tiraidis, C. / Zographos, S.E. / Gyorgydeak, Z. / Somsak, L. / Docsa, T. ...Anagnostou, E. / Kosmopoulou, M.N. / Chrysina, E.D. / Leonidas, D.D. / Hadjiloi, T. / Tiraidis, C. / Zographos, S.E. / Gyorgydeak, Z. / Somsak, L. / Docsa, T. / Gergely, P. / Kolisis, F.N. / Oikonomakos, N.G. | ||||||
![]() | ![]() Title: Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-d-glucopyranosylamine and N-trifluoroacetyl-beta-d-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase Authors: Anagnostou, E. / Kosmopoulou, M.N. / Chrysina, E.D. / Leonidas, D.D. / Hadjiloi, T. / Tiraidis, C. / Zographos, S.E. / Gyorgydeak, Z. / Somsak, L. / Docsa, T. / Gergely, P. / Kolisis, F.N. / Oikonomakos, N.G. #1: ![]() Title: N-acetyl-beta-D-glucopyranosylamine: a potent T-state inhibitor of glycogen phosphorylase. A comparison with alpha-D-glucose Authors: Oikonomakos, N.G. / Kontou, M. / Zographos, S.E. / Watson, K.A. / Johnson, L.N. / Bichard, C.J. / Fleet, G.W. / Acharya, K.R. #2: Journal: ACTA CRYSTALLOGR.,SECT.D / Year: 1995 Title: Glucose analogue inhibitors of glycogen phosphorylase: from crystallographic analysis to drug prediction using GRID force-field and GOLPE variable selection Authors: Watson, K.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 184.3 KB | Display | ![]() |
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PDB format | ![]() | 144.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 402.8 KB | Display | ![]() |
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Full document | ![]() | 417.4 KB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 29.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ww3C ![]() 2prjS 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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Details | Dimeric glycogen phosphorylase is the physiologiacally active species |
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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: Sugar | ChemComp-NBG / |
#3: Chemical | ChemComp-PLP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 48.91 % |
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Crystal grow | Temperature: 289 K / Method: small tubes / pH: 6.7 Details: 10mM Bes buffer, 3mM DDT, pH 6.7, SMALL TUBES, temperature 289K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 12, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→29.36 Å / Num. obs: 68661 / % possible obs: 89.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 22.6 Å2 / Rmerge(I) obs: 0.097 / Net I/σ(I): 6.6 |
Reflection shell | Resolution: 1.9→1.93 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.445 / Mean I/σ(I) obs: 2.4 / Num. unique all: 3387 / % possible all: 89.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2PRJ Resolution: 1.9→29.36 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 3297897 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 44.1731 Å2 / ksol: 0.311396 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→29.36 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.012 / Total num. of bins used: 6
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Xplor file |
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