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- PDB-1glb: STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1glb | ||||||
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Title | STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE | ||||||
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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 | ![]() | ||||||
![]() | Hurley, J.H. / Worthylake, D. / Faber, H.R. / Meadow, N.D. / Roseman, S. / Pettigrew, D.W. / Remington, S.J. | ||||||
![]() | ![]() Title: Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Authors: Hurley, J.H. / Faber, H.R. / Worthylake, D. / Meadow, N.D. / Roseman, S. / Pettigrew, D.W. / Remington, S.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137 KB | Display | ![]() |
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PDB format | ![]() | 105.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 469.3 KB | Display | ![]() |
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Full document | ![]() | 489.1 KB | Display | |
Data in XML | ![]() | 15.9 KB | Display | |
Data in CIF | ![]() | 23.7 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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Unit cell |
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Details | GLYCEROL KINASE EXISTS AT PHYSIOLOGICAL CONCENTRATIONS IN AN EQUILIBRIUM BETWEEN FUNCTIONAL DIMERS AND TETRAMERS. THE CRYSTAL CONTAINS TETRAMERS OF GLYCEROL-GLUCOSE-SPECIFIC FACTOR III COMPLEX KINASE WITH EXACT 222 POINT-GROUP SYMMETRY. THE TETRAMER IS LOCATED AT THE INTERSECTION OF THREE TWO-FOLD AXES IN THE CRYSTAL LATTICE. 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 0.0 124.90 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 0.0 124.90 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
#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.) ![]() ![]() |
#3: Chemical | ChemComp-ADP / |
#4: Chemical | ChemComp-GOL / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.49 Å3/Da / Density % sol: 64.73 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6 / Method: vapor diffusion | ||||||||||||||||||||||||||||||
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 |
Reflection | *PLUS Highest resolution: 2.6 Å / Num. obs: 24169 / % possible obs: 76 % / Num. measured all: 81994 / Rmerge(I) obs: 0.056 |
Reflection shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.7 Å / Num. possible: 58 / Rmerge(I) obs: 0.232 |
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Processing
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Refinement | Rfactor Rwork: 0.205 / Rfactor obs: 0.205 / Highest resolution: 2.6 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.6 Å
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Refine LS restraints |
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