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- PDB-1glc: CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1glc | ||||||
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Title | CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION | ||||||
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![]() | PHOSPHOTRANSFERASE | ||||||
Function / homology | ![]() negative regulation of carbohydrate metabolic process / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / glycerol kinase / glycerol-3-phosphate biosynthetic process / glycerol kinase activity / glycerol metabolic process / phosphoenolpyruvate-dependent sugar phosphotransferase system / glycerol catabolic process ...negative regulation of carbohydrate metabolic process / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / glycerol kinase / glycerol-3-phosphate biosynthetic process / glycerol kinase activity / glycerol metabolic process / phosphoenolpyruvate-dependent sugar phosphotransferase system / glycerol catabolic process / triglyceride metabolic process / transmembrane transporter complex / kinase activity / phosphorylation / DNA damage response / zinc ion binding / ATP binding / identical protein binding / membrane / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Feese, M.D. / Meadow, N.D. / Roseman, S. / Pettigrew, D.W. / Remington, S.J. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 140.6 KB | Display | ![]() |
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PDB format | ![]() | 106.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 477.9 KB | Display | ![]() |
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Full document | ![]() | 537 KB | Display | |
Data in XML | ![]() | 22.2 KB | Display | |
Data in CIF | ![]() | 32.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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 0.0 125.16 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 0.0 125.16 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 |
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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.) ![]() ![]() 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.) ![]() ![]() |
-Non-polymers , 5 types, 46 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/G3H.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/G3H.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-ZN / |
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#4: Chemical | ChemComp-MG / |
#5: Chemical | ChemComp-G3H / |
#6: Chemical | ChemComp-ADP / |
#7: Water | ChemComp-HOH / |
-Details
Nonpolymer details | THE COMPLEX OF GLYCEROL KINASE AND III-GLC CREATES AN INTERMOLECULAR ZINC BINDING SITE. HISTIDINES ...THE COMPLEX OF GLYCEROL KINASE AND III-GLC CREATES AN INTERMOLEC |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.48 Å3/Da / Density % sol: 64.66 % | ||||||||||||||||||||||||||||||
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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 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.65→14.5 Å / Rfactor obs: 0.166 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.65→14.5 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.166 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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