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- PDB-1ygp: PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHAT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ygp | ||||||
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Title | PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE. | ||||||
![]() | YEAST GLYCOGEN PHOSPHORYLASE | ||||||
![]() | GLYCOSYLTRANSFERASE / YEAST / PHOSPHORYLATED FORM | ||||||
Function / homology | ![]() Glycogen breakdown (glycogenolysis) / glycogen phosphorylase / glycogen phosphorylase activity / linear malto-oligosaccharide phosphorylase activity / SHG alpha-glucan phosphorylase activity / glycogen catabolic process / Neutrophil degranulation / pyridoxal phosphate binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lin, K. / Rath, V.L. / Dai, S.C. / Fletterick, R.J. / Hwang, P.K. | ||||||
![]() | ![]() Title: A protein phosphorylation switch at the conserved allosteric site in GP. Authors: Lin, K. / Rath, V.L. / Dai, S.C. / Fletterick, R.J. / Hwang, P.K. #1: ![]() Title: Mechanism of Regulation in Yeast Glycogen Phosphorylase Authors: Lin, K. / Hwang, P.K. / Fletterick, R.J. #2: ![]() Title: Parallel Evolution in Two Homologues of Phosphorylase Authors: Rath, V.L. / Fletterick, R.J. #3: ![]() Title: Purification and Crystallization of Glycogen Phosphorylase from Saccharomyces Cerevisiae Authors: Rath, V.L. / Hwang, P.K. / Fletterick, R.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 352.6 KB | Display | ![]() |
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PDB format | ![]() | 277.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421 KB | Display | ![]() |
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Full document | ![]() | 500.1 KB | Display | |
Data in XML | ![]() | 45 KB | Display | |
Data in CIF | ![]() | 63.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.756, 0.22, -0.617), Vector: Details | THE AUTHORS ONLY DEPOSITED ONE CHAIN. THE PDB GENERATED THE SECOND CHAIN IN THE ASYMMETRIC UNIT FROM THE CHAIN THAT WAS DEPOSITED USING THE TRANSFORMATION ON MTRIX RECORDS BELOW. | |
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Components
#1: Protein | Mass: 101278.820 Da / Num. of mol.: 2 / Mutation: N-TERMINAL 22 RESIDUE DELETION Source method: isolated from a genetically manipulated source Details: PHOSPHORYLATED FORM OF THE ENZYME Source: (gene. exp.) ![]() ![]() Gene: YEAST GLYCOGEN PHOSPHORYLASE / Organ: TAIL / Plasmid: PTACTAC / Gene (production host): YEAST GLYCOGEN PHOSPHORYLASE / Production host: ![]() ![]() #2: Chemical | ChemComp-PO4 / #3: Chemical | Sequence details | THE NUMBERING OF RESIDUES IS RELATIVE TO THE MAMMALIAN GLYCOGEN PHOSPHORYLASE SEQUENCE. THE LONGER ...THE NUMBERING OF RESIDUES IS RELATIVE TO THE MAMMALIAN GLYCOGEN PHOSPHORYL | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 6 / Method: vapor diffusion, hanging dropDetails: used to seeding, Lin, K., (1997) Structure, 5, 1511. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Apr 8, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 50707 / % possible obs: 72 % / Observed criterion σ(I): 1.5 / Redundancy: 5 % / Rmerge(I) obs: 0.105 |
Reflection | *PLUS Highest resolution: 2.8 Å / Num. measured all: 247322 |
Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 3 Å / Redundancy: 0.043 % |
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Processing
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Refinement | Resolution: 2.8→6 Å / σ(F): 2 Details: RESIDUE PHE 750 IS AT THE BEGINNING OF A BROKEN LOOP FOR WHICH THE ELECTRON DENSITY IS POOR. IT HAS A BAD PHI/PSI ANGLE, AND SHOULD BE IGNORED.
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Refinement step | Cycle: LAST / Resolution: 2.8→6 Å
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Refine LS restraints |
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Xplor file |
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