+Open data
-Basic information
Entry | Database: PDB / ID: 1z6p | ||||||
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Title | Glycogen phosphorylase AMP site inhibitor complex | ||||||
Components | Glycogen phosphorylase, muscle form | ||||||
Keywords | TRANSFERASE / GLYCOGEN METABOLISM / GLYCOGEN PHOSPHORYLASE B / INHIBITION / allosteric | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Kristiansen, M. / Andersen, B. / Iversen, L.F. / Westergaard, N. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2004 Title: Identification, synthesis and chracterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site Authors: Kristiansen, M. / Andersen, B. / Iversen, L.F. / Westergaard, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z6p.cif.gz | 174.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z6p.ent.gz | 143.2 KB | Display | PDB format |
PDBx/mmJSON format | 1z6p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1z6p_validation.pdf.gz | 474.1 KB | Display | wwPDB validaton report |
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Full document | 1z6p_full_validation.pdf.gz | 509.9 KB | Display | |
Data in XML | 1z6p_validation.xml.gz | 22.5 KB | Display | |
Data in CIF | 1z6p_validation.cif.gz | 32.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z6/1z6p ftp://data.pdbj.org/pub/pdb/validation_reports/z6/1z6p | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 97519.320 Da / Num. of mol.: 1 / Fragment: Glycogen Phosphorylase / Source method: isolated from a natural source / Details: gene PYGM / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: muscle / References: UniProt: P00489, glycogen phosphorylase |
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#2: Chemical | ChemComp-194 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 50 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7 Details: BES, EDTA. DTT, SPERMINE, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 2, 1999 |
Radiation | Monochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. all: 36575 / Num. obs: 36575 / % possible obs: 97 % / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.4→2.44 Å / % possible all: 48 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→20 Å / Cross valid method: THROUGHOUT / σ(F): 3 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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