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Open data
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Basic information
Entry | Database: PDB / ID: 5ta0 | |||||||||
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Title | Crystal structure of BuGH86E322Q in complex with neoagarooctaose | |||||||||
![]() | Glycoside Hydrolase | |||||||||
![]() | HYDROLASE / (alpha/beta)6 barrel / glycoside hydrolase | |||||||||
Function / homology | ![]() Jelly Rolls - #1200 / Porphyranase catalytic subdomain 1 / Beta-porphyranase A, C-terminal / beta porphyranase A C-terminal / Porphyranase catalytic subdomain 1 / Glycoside hydrolase superfamily / Jelly Rolls / Sandwich / Mainly Beta Similarity search - Domain/homology | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() ![]() | |||||||||
![]() | Pluvinage, B. / Boraston, A.B. / Abbott, W.D. | |||||||||
![]() | ![]() Title: Molecular basis of an agarose metabolic pathway acquired by a human intestinal symbiont. Authors: Pluvinage, B. / Grondin, J.M. / Amundsen, C. / Klassen, L. / Moote, P.E. / Xiao, Y. / Thomas, D. / Pudlo, N.A. / Anele, A. / Martens, E.C. / Inglis, G.D. / Uwiera, R.E.R. / Boraston, A.B. / Abbott, D.W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 307 KB | Display | ![]() |
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PDB format | ![]() | 248.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 781.3 KB | Display | ![]() |
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Full document | ![]() | 792.4 KB | Display | |
Data in XML | ![]() | 59.4 KB | Display | |
Data in CIF | ![]() | 91 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5t98C ![]() 5t99C ![]() 5t9aC ![]() 5t9gC ![]() 5t9xC ![]() 5ta1C ![]() 5ta5C ![]() 5ta7C ![]() 5ta9C 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
-Protein / Sugars , 2 types, 3 molecules AB
#1: Protein | Mass: 74747.688 Da / Num. of mol.: 2 / Mutation: E322Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Polysaccharide | beta-D-galactopyranose-(1-4)-3,6-anhydro-alpha-L-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)- ...beta-D-galactopyranose-(1-4)-3,6-anhydro-alpha-L-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)-3,6-anhydro-alpha-L-galactopyranose-(1-3)-beta-D-galactopyranose | Source method: isolated from a genetically manipulated source |
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-Non-polymers , 5 types, 1363 molecules ![](data/chem/img/SO4.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-EDO / #5: Chemical | ChemComp-GOL / #6: Chemical | ChemComp-CA / #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.72 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: 0.16M CaOAc, 0.1M Na cacodylate, 17.5% PEG 8000, 5% glycerol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Mar 18, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.984 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→85.9 Å / Num. obs: 256936 / % possible obs: 95.7 % / Redundancy: 6.6 % / CC1/2: 0.998 / Rmerge(I) obs: 0.07 / Net I/σ(I): 15.7 |
Reflection shell | Resolution: 1.4→1.48 Å / Redundancy: 6.6 % / Rmerge(I) obs: 0.324 / Mean I/σ(I) obs: 5.4 / CC1/2: 0.952 / % possible all: 93.4 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 70.9 Å2 / Biso mean: 13.685 Å2 / Biso min: 4.76 Å2
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Refinement step | Cycle: final / Resolution: 1.4→82.88 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.4→1.436 Å / Total num. of bins used: 20
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