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Yorodumi- PDB-1noi: COMPLEX OF GLYCOGEN PHOSPHORYLASE WITH A TRANSITION STATE ANALOGU... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1noi | ||||||
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Title | COMPLEX OF GLYCOGEN PHOSPHORYLASE WITH A TRANSITION STATE ANALOGUE NOJIRIMYCIN TETRAZOLE AND PHOSPHATE IN THE T AND R STATES | ||||||
Components | GLYCOGEN PHOSPHORYLASE | ||||||
Keywords | GLYCOGEN PHOSPHORYLASE / TRANSFERASE / GLYCOSYLTRANSFERASE | ||||||
Function / homology | Function and homology information 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 | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.5 Å | ||||||
Authors | Johnson, L.N. / Mitchell, E.P. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states. Authors: Mitchell, E.P. / Withers, S.G. / Ermert, P. / Vasella, A.T. / Garman, E.F. / Oikonomakos, N.G. / Johnson, L.N. #1: Journal: Helv.Chim.Acta / Year: 1991 Title: Synthesis of a Glucose Derived Tetrazole as a New Beta-Glucosidase Inhibitor Authors: Ermert, P. / Vasella, A.T. #2: Journal: Nature / Year: 1989 Title: The Allosteric Transition of Glycogen Phosphorylase Authors: Barford, D. / Johnson, L.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1noi.cif.gz | 676.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1noi.ent.gz | 569.3 KB | Display | PDB format |
PDBx/mmJSON format | 1noi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/no/1noi ftp://data.pdbj.org/pub/pdb/validation_reports/no/1noi | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 97317.242 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: MUSCLESkeletal muscle / References: UniProt: P00489, glycogen phosphorylase #2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-PLP / #4: Chemical | ChemComp-NTZ / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 55 % | |||||||||||||||||||||||||||||||||||
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Crystal | *PLUS | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.7 / Method: unknown | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.5 / Wavelength: 0.9 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Num. obs: 107826 / % possible obs: 88 % / Observed criterion σ(I): 3 / Redundancy: 2.4 % / Rmerge(I) obs: 0.07 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 9999 Å / Num. measured all: 263189 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.56 Å / % possible obs: 74 % |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 34.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Xplor file |
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