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Yorodumi- PDB-1gle: CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gle | ||||||
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Title | CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION | ||||||
Components |
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Keywords | PHOSPHOTRANSFERASE | ||||||
Function / homology | Function and homology information negative regulation of carbohydrate metabolic process / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / glycerol kinase / glycerol kinase activity / glycerol-3-phosphate metabolic process / glycerol metabolic process / glycerol catabolic process / phosphoenolpyruvate-dependent sugar phosphotransferase system ...negative regulation of carbohydrate metabolic process / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / glycerol kinase / glycerol kinase activity / glycerol-3-phosphate metabolic process / glycerol metabolic process / glycerol catabolic process / phosphoenolpyruvate-dependent sugar phosphotransferase system / transmembrane transporter complex / kinase activity / phosphorylation / DNA damage response / zinc ion binding / ATP binding / membrane / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.94 Å | ||||||
Authors | Feese, M.D. / Meadow, N.D. / Roseman, S. / Pettigrew, D.W. / Remington, S.J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Authors: Feese, M. / Pettigrew, D.W. / Meadow, N.D. / Roseman, S. / Remington, S.J. #1: Journal: Science / Year: 1993 Title: Three-Dimensional Structure of the Regulatory Complex of Escherichia Coli III-Glc with Glycerol Kinase Authors: Hurley, J.H. / Worthylake, D. / Faber, H.R. / Meadow, N.D. / Roseman, S. / Pettigrew, D.W. / Remington, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gle.cif.gz | 139.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gle.ent.gz | 105.9 KB | Display | PDB format |
PDBx/mmJSON format | 1gle.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gl/1gle ftp://data.pdbj.org/pub/pdb/validation_reports/gl/1gle | 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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Atom site foot note | 1: CIS PROLINE - PRO G 354 | ||||||||
Details | THE CRYSTAL CONTAINS TETRAMERS OF THE GLYCEROL KINASE/III-GLC COMPLEX WITH 222 POINT-GROUP SYMMETRY. THE TETRAMER IS LOCATED AT THE INTERSECTION OF THREE CRYSTALLOGRAPHIC TWO-FOLD AXES. THE FOLLOWING TRANSFORMATIONS WILL PRODUCE A TETRAMER OF THE COMPLEX WHEN APPLIED TO THE COORDINATES IN THIS ENTRY: TRANSFORM 1 (-X, 1-Y, Z) -1.0 0.0 0.0 0.0 0.0 -1.0 0.0 125.11 0.0 0.0 1.0 0.0 TRANSFORM 2 ( X, 1-Y, -Z) 1.0 0.0 0.0 0.0 0.0 -1.0 0.0 125.11 0.0 0.0 1.0 0.0 TRANSFORM 3 (-X, Y, -Z) -1.0 0.0 0.0 0.0 0.0 1.0 0.0 0.0 0.0 0.0 -1.0 0.0 |
-Components
-Protein , 2 types, 2 molecules FG
#1: Protein | Mass: 18141.834 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) References: UniProt: P69783, protein-Npi-phosphohistidine-sugar phosphotransferase |
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#2: Protein | Mass: 56162.352 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0A6F3, glycerol kinase |
-Non-polymers , 4 types, 52 molecules
#3: Chemical | #4: Chemical | ChemComp-G3H / | #5: Chemical | ChemComp-ADP / | #6: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | A ZN(II) ALSO BINDS AT THE ACTIVE SITE OF GLYCEROL KINASE BETWEEN THE PHOSPHORYL OXYGENS OF ADP AND ...A ZN(II) ALSO BINDS AT THE ACTIVE SITE OF GLYCEROL KINASE BETWEEN THE PHOSPHORYL |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.48 Å3/Da / Density % sol: 64.65 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.1 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.94→21.8 Å / Rfactor obs: 0.149 / σ(F): 0 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.94→21.8 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.149 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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