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Yorodumi- PDB-1fba: THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fba | ||||||
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Title | THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION | ||||||
Components | FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE | ||||||
Keywords | LYASE(ALDEHYDE) | ||||||
Function / homology | Function and homology information Fructose catabolism / Glycolysis / Gluconeogenesis / Platelet degranulation / Neutrophil degranulation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / fructose 1,6-bisphosphate metabolic process / mesoderm development ...Fructose catabolism / Glycolysis / Gluconeogenesis / Platelet degranulation / Neutrophil degranulation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / fructose 1,6-bisphosphate metabolic process / mesoderm development / glycolytic process / Z disc / glucose homeostasis / cytosol Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Piontek, K. / Hester, G. / Brenner-Holzach, O. | ||||||
Citation | Journal: FEBS Lett. / Year: 1991 Title: The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution. Authors: Hester, G. / Brenner-Holzach, O. / Rossi, F.A. / Struck-Donatz, M. / Winterhalter, K.H. / Smit, J.D. / Piontek, K. #1: Journal: Arch.Biochem.Biophys. / Year: 1988 Title: Fructose-1,6-Bisphosphate Aldolase from Drosophila Melanogaster: Primary Structure Analysis, Secondary Structure Prediction, and Comparison with Vertebrate Aldolases Authors: Malek, A.A. / Hy, M. / Honegger, A. / Rose, K. / Brenner-Holzach, O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fba.cif.gz | 312.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fba.ent.gz | 251.8 KB | Display | PDB format |
PDBx/mmJSON format | 1fba.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fba_validation.pdf.gz | 441.2 KB | Display | wwPDB validaton report |
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Full document | 1fba_full_validation.pdf.gz | 469.6 KB | Display | |
Data in XML | 1fba_validation.xml.gz | 72.7 KB | Display | |
Data in CIF | 1fba_validation.cif.gz | 108.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fb/1fba ftp://data.pdbj.org/pub/pdb/validation_reports/fb/1fba | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE 158 IS A CIS PROLINE IN ALL FOUR CHAINS. | ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 38989.180 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / References: UniProt: P07764, fructose-bisphosphate aldolase #2: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE IS DESCRIBED IN REFERENCE 1 ABOVE. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.94 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 2-4 ℃ / pH: 7.8 / Method: vapor diffusion, hanging drop / Details: referred to J.Biol.Chem. 257.11747-11749 1987 | |||||||||||||||||||||||||||||||||||||||||||||
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: 1.9 Å / Lowest resolution: 30 Å / Num. obs: 123654 / % possible obs: 87 % / Num. measured all: 377901 / Rmerge(I) obs: 0.097 |
-Processing
Software |
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Refinement | Resolution: 1.9→8 Å / Rfactor obs: 0.179 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 8 Å / Rfactor obs: 0.179 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 0.021 |