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Open data
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Basic information
Entry | Database: PDB / ID: 6ald | ||||||
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Title | RABBIT MUSCLE ALDOLASE A/FRUCTOSE-1,6-BISPHOSPHATE COMPLEX | ||||||
![]() | FRUCTOSE-1,6-BIS(PHOSPHATE) ALDOLASE | ||||||
![]() | LYASE / ALDOLASE A / FRUCTOSE-1 / 6-BISPHOSPHATE / LINEAR HEXOSE / MICHAELIS COMPLEX | ||||||
Function / homology | ![]() negative regulation of Arp2/3 complex-mediated actin nucleation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / I band / fructose 1,6-bisphosphate metabolic process / glycolytic process / protein homotetramerization / positive regulation of cell migration / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Choi, K.H. / Mazurkie, A.S. / Morris, A.J. / Utheza, D. / Tolan, D.R. / Allen, K.N. | ||||||
![]() | ![]() Title: Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,). Authors: Choi, K.H. / Mazurkie, A.S. / Morris, A.J. / Utheza, D. / 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 | ![]() | 270.4 KB | Display | ![]() |
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PDB format | ![]() | 219.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 877.1 KB | Display | ![]() |
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Full document | ![]() | 919.1 KB | Display | |
Data in XML | ![]() | 56.4 KB | Display | |
Data in CIF | ![]() | 77.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1adoS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 39205.570 Da / Num. of mol.: 4 / Mutation: K146A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Sugar | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.4 / Details: pH 7.4 | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Dec 1, 1997 / Details: SUPER LONG MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→100 Å / Num. obs: 62360 / % possible obs: 94.5 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.179 / Rsym value: 0.179 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 3 % / Rmerge(I) obs: 0.459 / Mean I/σ(I) obs: 2.43 / % possible all: 74 |
Reflection | *PLUS Rmerge(I) obs: 0.092 |
Reflection shell | *PLUS % possible obs: 95.3 % / Rmerge(I) obs: 0.182 / Mean I/σ(I) obs: 2.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ADO Resolution: 2.3→100 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 26.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→100 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.3→2.4 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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