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- PDB-2bi7: udp-galactopyranose mutase from Klebsiella pneumoniae oxidised FAD -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bi7 | |||||||||
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Title | udp-galactopyranose mutase from Klebsiella pneumoniae oxidised FAD | |||||||||
![]() | UDP-GALACTOPYRANOSE MUTASE | |||||||||
![]() | ISOMERASE / FAD / FLAVOPROTEIN / LIPOPOLYSACCHARIDE BIOSYNTHESIS | |||||||||
Function / homology | ![]() UDP-galactopyranose mutase / UDP-galactopyranose mutase activity / O antigen biosynthetic process / flavin adenine dinucleotide binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Beis, K. / Srikannathasan, V. / Naismith, J. | |||||||||
![]() | ![]() Title: Crystal Structures of Mycobacteria Tuberculosis and Klebsiella Pneumoniae Udp-Galactopyranose Mutase in the Oxidised State and Klebsiella Pneumoniae Udp-Galactopyranose Mutase in the (Active) Reduced State. Authors: Beis, K. / Srikannathasan, V. / Liu, H. / Fullerton, S.W.B. / Bamford, V.A. / Sanders, D.A.R. / Whitfield, C. / Mcneil, M.R. / Naismith, J.H. #1: ![]() Title: Udp-Galactopyranose Mutase Has a Novel Structure and Mechanism Authors: Sanders, D.A. / Staines, A.G. / Mcmahon, S.A. / Mcneil, M.R. / Whitfield, C. / Naismith, J.H. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95.5 KB | Display | ![]() |
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PDB format | ![]() | 71.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 689.2 KB | Display | ![]() |
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Full document | ![]() | 694 KB | Display | |
Data in XML | ![]() | 17.5 KB | Display | |
Data in CIF | ![]() | 24.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1v0jC ![]() 1wamC ![]() 2bi8C ![]() 1i8tS C: citing same article ( 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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Components
#1: Protein | Mass: 44512.180 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FAD / |
#3: Water | ChemComp-HOH / |
Compound details | FUNCTION: INVOLVED IN THE CONVERSION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47 % |
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Crystal grow | pH: 6.5 Details: 0.1M BIS-TRIS PH6.5, 50MM CACL2, 30% PEG550, pH 6.50 |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 15, 2003 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→74.54 Å / Num. obs: 2160 / % possible obs: 98.1 % / Redundancy: 16.6 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 10.6 |
Reflection shell | Resolution: 2→2.12 Å / Redundancy: 9.1 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 4.3 / % possible all: 88.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1I8T Resolution: 2→74.54 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.926 / SU ML: 0.127 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.223 / ESU R Free: 0.194 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.83 Å2
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Refinement step | Cycle: LAST / Resolution: 2→74.54 Å
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Refine LS restraints |
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