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- PDB-1tip: THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tip | ||||||
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Title | THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE | ||||||
![]() | PHOSPHOENZYME INTERMEDIATE OF FRU-2,6-BISPHOSPHATASE | ||||||
![]() | HYDROLASE / MULTIFUNCTIONAL ENZYME / TRANSFERASE / KINASE / ATP-BINDING / PHOSPHORYLATION / ALTERNATIVE SPLICING / MULTIGENE FAMILY | ||||||
Function / homology | ![]() positive regulation of glycolytic process through fructose-6-phosphate / 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / 6-phosphofructo-2-kinase / 6-phosphofructo-2-kinase activity / fructose 2,6-bisphosphate metabolic process / fructose-2,6-bisphosphate 2-phosphatase / fructose-2,6-bisphosphate 2-phosphatase activity / fructose-6-phosphate binding / carbohydrate phosphorylation ...positive regulation of glycolytic process through fructose-6-phosphate / 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / 6-phosphofructo-2-kinase / 6-phosphofructo-2-kinase activity / fructose 2,6-bisphosphate metabolic process / fructose-2,6-bisphosphate 2-phosphatase / fructose-2,6-bisphosphate 2-phosphatase activity / fructose-6-phosphate binding / carbohydrate phosphorylation / fructose metabolic process / response to glucagon / negative regulation of glycolytic process through fructose-6-phosphate / response to starvation / animal organ regeneration / response to glucocorticoid / response to cAMP / kinase binding / response to insulin / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lee, Y.-H. / Olson, T.W. / Ogata, C.M. / Levitt, D.G. / Banaszak, L.J. / Lange, A.J. | ||||||
![]() | ![]() Title: Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Authors: Lee, Y.H. / Olson, T.W. / Ogata, C.M. / Levitt, D.G. / Banaszak, L.J. / Lange, A.J. #1: ![]() Title: 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase: A Metabolic Signaling Enzyme Authors: Pilkis, S.J. / Claus, T.H. / Kurland, I.J. / Lange, A.J. #2: ![]() Title: Preliminary X-Ray Analysis of a Truncated Form of Recombinant Fructose-2,6-Bisphosphatase Authors: Lee, Y.H. / Lin, K. / Okar, D. / Alfano, N.L. / Sarma, R. / Pflugrath, J.W. / Pilkis, S.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 92.4 KB | Display | ![]() |
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PDB format | ![]() | 73.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: (-0.999546, -0.029783, -0.004615), Vector: |
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Components
#1: Protein | Mass: 22258.334 Da / Num. of mol.: 2 / Mutation: 30 C-TERMINAL AMINO ACIDS DELETED Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene (production host): A CODING REGION WHICH COVERS FRUCTOSE-2,6-BISPHOSPHATASE DOMAIN (RESIDUES 251 - 440) OF THE RAT LIVER 6-PF-2-K/FRU-2,6-P2ASE (RESIDUES 1 - 470) Production host: ![]() ![]() References: UniProt: P07953, fructose-2,6-bisphosphate 2-phosphatase #2: Sugar | #3: Water | ChemComp-HOH / | Nonpolymer details | A COMPETITIVE INHIBITOR, PHOSPHATE, WAS USED FOR THE CRYSTALLIZATION BUFFER. THE PRESENCE OF PI IN ...A COMPETITIV | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 52 % / Description: NUMBER OF CRYSTALS 1. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Details: A CATALYTIC PHOSPHOSENZYME INTERMEDIATE STATE OF THE BISPHOSPHATASE WAS PREPARED BY SOAKING OF THE NATIVE CRYSTAL OF THE PROTEIN AND TRAPPED USING THE CRYOGENIC DEVICE. A 2.2 ANGSTROM ...Details: A CATALYTIC PHOSPHOSENZYME INTERMEDIATE STATE OF THE BISPHOSPHATASE WAS PREPARED BY SOAKING OF THE NATIVE CRYSTAL OF THE PROTEIN AND TRAPPED USING THE CRYOGENIC DEVICE. A 2.2 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE INTERMEDIATE WAS DETERMINED. A PHOSPHORYLATED CATALYTIC HISTIDINE WAS VISUALIZED ALONG WITH THE FIRST PRODUCT, FRUCTOSE-6 - PHOSPHATE, AND THE CATALYTIC WATER, SHOWING THE COMPREHENSIVE GEOMETRY OF A TRIGONAL BI-PYRAMIDAL STRUCTURE. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop / Details: Lee, Y.H., (1996) Biochemistry, 35, 6010. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: May 5, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.02 Å / Relative weight: 1 |
Reflection | Num. obs: 20142 / % possible obs: 78.3 % / Observed criterion σ(I): 3 / Redundancy: 8.9 % / Rmerge(I) obs: 0.052 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 20 Å / Rmerge(I) obs: 0.033 |
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Processing
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Refinement | Resolution: 2.2→20 Å / σ(F): 0
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Displacement parameters | Biso mean: 27.94 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 27.942 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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