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- PDB-3int: Structure of UDP-galactopyranose mutase bound to UDP-galactose (r... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3int | ||||||
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Title | Structure of UDP-galactopyranose mutase bound to UDP-galactose (reduced) | ||||||
![]() | Probable UDP-galactopyranose mutase | ||||||
![]() | ISOMERASE / Flavoenzyme / protein-ligand complex / carbohydrate biosynthesis / 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 | ![]() ![]() ![]() | ||||||
![]() | Gruber, T.D. / Kiessling, L.L. / Forest, K.T. | ||||||
![]() | ![]() Title: X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin . Authors: Gruber, T.D. / Westler, W.M. / Kiessling, L.L. / Forest, K.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 175.4 KB | Display | ![]() |
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PDB format | ![]() | 137.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3inrC ![]() 3gf4S 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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Unit cell |
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Components
#1: Protein | Mass: 45237.945 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: C-terminal Arg384 was altered to glycine during cloning, and six histidine residues were engineered on the C-terminus as a tag. Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-UDP / | #4: Chemical | ChemComp-GDU / | #5: Water | ChemComp-HOH / | Sequence details | THESE ARE VERY CONSERVATIVE MUTATIONS FROM THE PUBLISHED SEQUENCE. THEY REFLECT SEQUENCE ...THESE ARE VERY CONSERVATI | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.17 Å3/Da / Density % sol: 61.15 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: Drops containing 1.5 microliters 5 mg/mL protein in 20 mM HEPES were combined with 1.5 microliters well solution (85 mM ammonium acetate, 42 mM tri-sodium citrate, 12.3% PEG 4000, 7.5% ...Details: Drops containing 1.5 microliters 5 mg/mL protein in 20 mM HEPES were combined with 1.5 microliters well solution (85 mM ammonium acetate, 42 mM tri-sodium citrate, 12.3% PEG 4000, 7.5% glycerol, 15 mM L-cysteine, 5 mM UDP-Glc) for 1-2 weeks. Crystals were then soaked in a solution of 53% Qiagen Cryos Suite Condition #87 with 15 mM L-cys, 30% methanol, 90 mM UDP-Galp (24hrs). Crystals were then soaked in a solution of 53% Qiagen Cryos Suite Condition #87 with 15 mM L-cys, 30% methanol, 90 mM UDP-Galp plus 100 mM sodium dithionite (3 min), pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 5, 2008 / Details: Beryllium lens |
Radiation | Monochromator: C(111) diamond laue / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. all: 38556 / Num. obs: 38510 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.6 % / Rsym value: 0.107 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 7.5 % / Mean I/σ(I) obs: 6.7 / Rsym value: 0.329 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3GF4 Resolution: 2.51→30 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.917 / SU B: 8.461 / SU ML: 0.19 / Cross valid method: THROUGHOUT / ESU R: 0.391 / ESU R Free: 0.267 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 43.795 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.51→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.51→2.57 Å / Total num. of bins used: 20
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