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Open data
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Basic information
Entry | Database: PDB / ID: 1x8f | ||||||
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Title | Crystal Structure Of apo-Kdo8P Synthase | ||||||
![]() | 2-dehydro-3-deoxyphosphooctonate aldolase | ||||||
![]() | TRANSFERASE / BETA-ALPHA-BARRELS / LYASE / LIPOPOLYSACCHARIDE | ||||||
Function / homology | ![]() 3-deoxy-8-phosphooctulonate synthase / 3-deoxy-8-phosphooctulonate synthase activity / keto-3-deoxy-D-manno-octulosonic acid biosynthetic process / protein-containing complex / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Vainer, R. / Belakhov, V. / Rabkin, E. / Baasov, T. / Adir, N. | ||||||
![]() | ![]() Title: Crystal Structures of Escherichia coli KDO8P Synthase Complexes Reveal the Source of Catalytic Irreversibility Authors: Vainer, R. / Belakhov, V. / Rabkin, E. / Baasov, T. / Adir, 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 | ![]() | 65.5 KB | Display | ![]() |
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PDB format | ![]() | 49.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 423.9 KB | Display | ![]() |
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Full document | ![]() | 441.9 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 19.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1phwSC ![]() 1q3nC ![]() 1x6uC S: Starting model for refinement C: citing same article ( |
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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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Unit cell |
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Details | The biological assembly is a tetramer generated from the monomer in the asymmetric unit by the operations: X,Y,Z -X,-Y,Z -X,Y,-Z X,-Y,-Z Z,X,Y Z,-X,-Y -Z,-X,Y -Z,X,-Y Y,Z,X -Y,Z,-X Y,-Z,-X -Y,-Z,X 1/2+X,1/2+Y,1/2+Z 1/2-X,1/2-Y,1/2+Z 1/2-X,1/2+Y,1/2-Z 1/2+X,1/2-Y,1/2-Z 1/2+Z,1/2+X,1/2+Y 1/2+Z,1/2-X,1/2-Y 1/2-Z,1/2-X,1/2+Y 1/2-Z,1/2+X,1/2-Y 1/2+Y,1/2+Z,1/2+X 1/2-Y,1/2+Z,1/2-X 1/2+Y,1/2-Z,1/2-X 1/2-Y,1/2-Z,1/2+X |
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Components
#1: Protein | Mass: 30870.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A715, 3-deoxy-8-phosphooctulonate synthase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 45.46 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG4000, tris-HCl, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 24, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. obs: 10401 / % possible obs: 100 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 3.5 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 2.4→2.49 Å / Rmerge(I) obs: 0.45 / Num. unique all: 647 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1PHW Resolution: 2.4→20 Å / Cross valid method: THROUGHOUT / σ(F): 4 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 72 Å2 | ||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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