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Open data
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Basic information
Entry | Database: PDB / ID: 1xfb | ||||||
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Title | Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme) | ||||||
![]() | Aldolase C | ||||||
![]() | LYASE / isozyme specificity / structural enzymology / protein-protein interactions / isozyme specific residues / structure/function | ||||||
Function / homology | ![]() neutrophil degranulation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / Gluconeogenesis / canonical glycolysis / fructose metabolic process / fructose 1,6-bisphosphate metabolic process / Glycolysis / epithelial cell differentiation / cytoskeletal protein binding ...neutrophil degranulation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / Gluconeogenesis / canonical glycolysis / fructose metabolic process / fructose 1,6-bisphosphate metabolic process / Glycolysis / epithelial cell differentiation / cytoskeletal protein binding / gluconeogenesis / glycolytic process / tertiary granule lumen / secretory granule lumen / ficolin-1-rich granule lumen / cytoskeleton / Neutrophil degranulation / extracellular exosome / extracellular region / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Arakaki, T.L. / Pezza, J.A. / Cronin, M.A. / Hopkins, C.E. / Zimmer, D.B. / Tolan, D.R. / Allen, K.N. | ||||||
![]() | ![]() Title: Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function Authors: Arakaki, T.L. / Pezza, J.A. / Cronin, M.A. / Hopkins, C.E. / Zimmer, D.B. / Tolan, D.R. / Allen, K.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 | ![]() | 678.9 KB | Display | ![]() |
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PDB format | ![]() | 578.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 514.7 KB | Display | ![]() |
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Full document | ![]() | 642.4 KB | Display | |
Data in XML | ![]() | 148.6 KB | Display | |
Data in CIF | ![]() | 196 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1j4eS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Details | Tetramer of molecules A, B, C, D / Tetramer of molecules E, F, G, H / Tetramer of molecules I, J, K, L |
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Components
#1: Protein | Mass: 39616.973 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG 8000, Calcium Acetate, Tris, glucose, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 1, 2003 / Details: osmic mirrors |
Radiation | Monochromator: osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→79.24 Å / Num. all: 89550 / Num. obs: 89550 / % possible obs: 97.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Limit h max: 27 / Limit h min: -29 / Limit k max: 41 / Limit k min: -29 / Limit l max: 46 / Limit l min: 0 / Observed criterion F max: 1989158.51 / Observed criterion F min: 6.4 / Rsym value: 0.097 / Net I/σ(I): 5.3 |
Reflection shell | Resolution: 3→3.15 Å / Mean I/σ(I) obs: 1.5 / Rsym value: 0.34 / % possible all: 95.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB Entry 1J4E Resolution: 3→79.24 Å / Rfactor Rfree error: 0.003 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: CNS bulk solvent model used / Bsol: 30.8274 Å2 / ksol: 0.370575 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 99.51 Å2 / Biso mean: 35.37 Å2 / Biso min: 0.51 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3→79.24 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 8
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Xplor file | Serial no: 1 / Param file: protein_rep.param / Topol file: protein.top |