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Yorodumi- PDB-2fbp: STRUCTURE REFINEMENT OF FRUCTOSE-1,6-BISPHOSPHATASE AND ITS FRUCT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fbp | ||||||
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Title | STRUCTURE REFINEMENT OF FRUCTOSE-1,6-BISPHOSPHATASE AND ITS FRUCTOSE 2,6-BISPHOSPHATE COMPLEX AT 2.8 ANGSTROMS RESOLUTION | ||||||
Components | FRUCTOSE 1,6-BISPHOSPHATASE | ||||||
Keywords | HYDROLASE (PHOSPHORIC MONOESTER) | ||||||
Function / homology | Function and homology information 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 | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Ke, H. / Thorpe, C.M. / Seaton, B.A. / Marcus, F. / Lipscomb, W.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1990 Title: Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution. Authors: Ke, H.M. / Thorpe, C.M. / Seaton, B. / Lipscomb, W.N. / Marcus, F. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1991 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. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1990 Title: Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose 6-Phosphate, AMP, and Magnesium Authors: Ke, H. / Zhang, Y. / Lipscomb, W.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fbp.cif.gz | 152.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fbp.ent.gz | 122.3 KB | Display | PDB format |
PDBx/mmJSON format | 2fbp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2fbp_validation.pdf.gz | 381.6 KB | Display | wwPDB validaton report |
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Full document | 2fbp_full_validation.pdf.gz | 430.2 KB | Display | |
Data in XML | 2fbp_validation.xml.gz | 18.8 KB | Display | |
Data in CIF | 2fbp_validation.cif.gz | 27.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fb/2fbp ftp://data.pdbj.org/pub/pdb/validation_reports/fb/2fbp | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 147, AND PRO B 147 ARE CIS PROLINES. ALSO SEE REMARK 5. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.23275, -0.41329, -0.88035), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. | |
-Components
#1: Protein | Mass: 36503.004 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P00636, fructose-bisphosphatase |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.71 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.4 / Method: microdialysis | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Num. obs: 16082 / % possible obs: 98 % / Num. measured all: 82889 / Rmerge(I) obs: 0.0598 |
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-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor Rwork: 0.194 / Highest resolution: 2.8 Å Details: PRO A 147 AND PRO B 147 HAS BEEN REFINED TO A TRANS CONFORMATION IN THE NEWLY REFINED 2.1 ANGSTROM STRUCTURE OF F6P COMPLEX (H. KE, Y.ZHANG, J.-Y. LIANG, AND W. N. LIPSCOMB (1991) PROC. NATL. ...Details: PRO A 147 AND PRO B 147 HAS BEEN REFINED TO A TRANS CONFORMATION IN THE NEWLY REFINED 2.1 ANGSTROM STRUCTURE OF F6P COMPLEX (H. KE, Y.ZHANG, J.-Y. LIANG, AND W. N. LIPSCOMB (1991) PROC. NATL. ACAD. SCI. 88, 2989-2993). | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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Refine LS restraints |
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Software | *PLUS Name: XPLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Rfactor obs: 0.194 / Lowest resolution: 10 Å / Num. reflection obs: 15079 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 36.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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