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- PDB-1fbh: CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fbh | |||||||||
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Title | CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | |||||||||
![]() | FRUCTOSE 1,6-BISPHOSPHATASE | |||||||||
![]() | HYDROLASE(PHOSPHORIC MONOESTER) | |||||||||
Function / homology | ![]() Gluconeogenesis / sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / cellular response to magnesium ion / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process / fructose metabolic process / monosaccharide binding / negative regulation of glycolytic process ...Gluconeogenesis / sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / cellular response to magnesium ion / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process / fructose metabolic process / monosaccharide binding / negative regulation of glycolytic process / fructose 1,6-bisphosphate metabolic process / regulation of gluconeogenesis / AMP binding / dephosphorylation / gluconeogenesis / negative regulation of cell growth / cellular response to xenobiotic stimulus / identical protein binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Zhang, Y. / Liang, J.-Y. / Huang, S. / Ke, H. / Lipscomb, W.N. | |||||||||
![]() | ![]() Title: Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Authors: Zhang, Y. / Liang, J.Y. / Huang, S. / Ke, H. / Lipscomb, W.N. #1: ![]() Title: Crystal Structure of the Neutral Form of Fructose-1,6-Bisphosphatase Complexed with the Product Fructose 6-Phosphate at 2.1 Angstroms Resolution Authors: Ke, H. / Zhang, Y. / Liang, J.-Y. / Lipscomb, W.N. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.1 KB | Display | ![]() |
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PDB format | ![]() | 129.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 613.4 KB | Display | ![]() |
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Full document | ![]() | 621.4 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 22.1 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.24574, -0.42562, -0.8709), Vector: Details | THE WHOLE MOLECULE IS A TETRAMER OF FOUR IDENTICAL CHAINS. THE OTHER HALF OF THE MOLECULE IS RELATED TO THE A + B DIMER BY A CRYSTALLOGRAPHIC TWO-FOLD OPERATION (Y, X, -Z). THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED TO CHAIN B. | |
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Components
#1: Protein | Mass: 36503.004 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Sugar | #3: Sugar | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.82 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.4 / Method: microdialysis | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 2.5 Å / Num. obs: 24277 / % possible obs: 91.2 % / Num. measured all: 94675 / Rmerge(I) obs: 0.077 |
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Processing
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Refinement | Rfactor Rwork: 0.193 / Rfactor obs: 0.193 / Highest resolution: 2.5 Å Details: THE SUBSTRATE AT THE ACTIVE SITE IS MODELED AS 20 PERCENT OF THE ALPHA ANOMER AND 80 PERCENT OF THE BETA ANOMER. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.193 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.7 |