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Yorodumi- PDB-1phk: TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1phk | ||||||
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Title | TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH NUCLEOTIDE, SUBSTRATE-ANALOGUE AND PRODUCT | ||||||
Components | PHOSPHORYLASE KINASE | ||||||
Keywords | KINASE / GLYCOGEN METABOLISM / TRANSFERASE / SERINE/THREONINE-PROTEIN / ATP-BINDING / CALMODULIN-BINDING | ||||||
Function / homology | Function and homology information phosphorylase kinase / phosphorylase kinase activity / phosphorylase kinase complex / tau-protein kinase / glycogen biosynthetic process / tau-protein kinase activity / skeletal muscle myofibril / calmodulin binding / non-specific serine/threonine protein kinase / phosphorylation ...phosphorylase kinase / phosphorylase kinase activity / phosphorylase kinase complex / tau-protein kinase / glycogen biosynthetic process / tau-protein kinase activity / skeletal muscle myofibril / calmodulin binding / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / ATP binding Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.2 Å | ||||||
Authors | Owen, D.J. / Noble, M.E.M. / Garman, E.F. / Papageorgiou, A.C. / Johnson, L.N. | ||||||
Citation | Journal: Structure / Year: 1995 Title: Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. Authors: Owen, D.J. / Noble, M.E. / Garman, E.F. / Papageorgiou, A.C. / Johnson, L.N. #1: Journal: J.Mol.Biol. / Year: 1995 Title: Expression, Purification and Crystallisation of Phosphorylase Kinase Catalytic Domain Authors: Owen, D.J. / Papageorgiou, A.C. / Garman, E.F. / Noble, M.E. / 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 | 1phk.cif.gz | 74.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1phk.ent.gz | 54 KB | Display | PDB format |
PDBx/mmJSON format | 1phk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ph/1phk ftp://data.pdbj.org/pub/pdb/validation_reports/ph/1phk | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 34316.297 Da / Num. of mol.: 1 / Fragment: GAMMA SUBUNIT, TRUNCATED TO RESIDUES 1 - 298 Source method: isolated from a genetically manipulated source Details: LIGANDS ATP AND MN(II) / Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Tissue: SKELETAL MUSCLE / Organ: SKELETALSkeleton / Plasmid: PMW172 / Production host: Escherichia coli (E. coli) / References: UniProt: P00518, EC: 2.7.1.38 | ||||
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#2: Chemical | #3: Chemical | ChemComp-ATP / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 14 ℃ / pH: 8.2 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.87 |
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Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 5, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.1 Å / Num. obs: 19961 / % possible obs: 88.8 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.074 |
-Processing
Software |
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Refinement | Resolution: 2.2→6 Å / σ(F): 2
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Displacement parameters | Biso mean: 47.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→6 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.21 / Rfactor Rwork: 0.21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |