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- PDB-1fbd: 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: 1fbd | ||||||
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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 | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() 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 | ![]() | 153.5 KB | Display | ![]() |
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PDB format | ![]() | 122.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: (-0.24534, -0.4243, -0.87165), 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: Chemical | ChemComp-MN / #3: Sugar | Nonpolymer details | THE SUBSTRATE ANALOGUE 2,5-ANHYDROGLUCITOL-1,6-BISPHOSPHATE OCCUPIES THE ACTIVE SITE OF THE A AND B ...THE SUBSTRATE ANALOGUE 2,5-ANHYDROGLU | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.38 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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: 2.9 Å / Num. obs: 11800 / % possible obs: 75.8 % / Num. measured all: 59064 / Rmerge(I) obs: 0.071 |
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Processing
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Refinement | Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.172 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.53 |