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Yorodumi- PDB-9ayu: Structure of the A type blood alpha-D-galactosamine galactosamini... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9ayu | ||||||
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| Title | Structure of the A type blood alpha-D-galactosamine galactosaminidase D463A mutant from Flavonifractor plautii | ||||||
Components | A type blood alpha-D-galactosamine galactosaminidase | ||||||
Keywords | SUGAR BINDING PROTEIN / galactosaminidase | ||||||
| Function / homology | Melibiase / : / alpha-galactosidase activity / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / Aldolase-type TIM barrel / Glycoside hydrolase superfamily / : / A type blood alpha-D-galactosamine galactosaminidase Function and homology information | ||||||
| Biological species | Flavonifractor plautii (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Worrall, L.J. / Strynadka, N.C.J. | ||||||
| Funding support | Canada, 1items
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Citation | Journal: Acs Catalysis / Year: 2024Title: Cobalt as a Cofactor for alpha-Galactosaminidase-Catalyzed Cleavage of Blood Group Antigens Authors: Tian, Y. / Worrall, L.J. / Sim, L. / Liu, F. / Nasseri, S.A. / Rahfeld, P. / Mu, W. / Kizhakkedathu, J.N. / Strynadka, N.C.J. / Withers, S.G. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9ayu.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ayu.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 9ayu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9ayu_validation.pdf.gz | 479.9 KB | Display | wwPDB validaton report |
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| Full document | 9ayu_full_validation.pdf.gz | 500.8 KB | Display | |
| Data in XML | 9ayu_validation.xml.gz | 163.6 KB | Display | |
| Data in CIF | 9ayu_validation.cif.gz | 229.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ay/9ayu ftp://data.pdbj.org/pub/pdb/validation_reports/ay/9ayu | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9awtC ![]() 9ay8C C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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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| 5 | ![]()
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| Unit cell |
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Components
-Protein , 1 types, 5 molecules ABCDE
| #1: Protein | Mass: 73569.141 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Flavonifractor plautii (bacteria) / Production host: ![]() References: UniProt: P0DTR5, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds |
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-Non-polymers , 5 types, 3107 molecules 








| #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-MN / #4: Chemical | ChemComp-CL / #5: Chemical | ChemComp-EDO / #6: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.01 Å3/Da / Density % sol: 59.15 % |
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| Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop Details: 0.2 M Sodium chloride, 0.1 M Tris pH 8, 20% (w/v) PEG 6000 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 1.0332 Å |
| Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 22, 2022 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
| Reflection | Resolution: 2→48.9 Å / Num. obs: 292440 / % possible obs: 100 % / Redundancy: 4.4 % / CC1/2: 0.992 / Rmerge(I) obs: 0.17 / Rpim(I) all: 0.09 / Rrim(I) all: 0.193 / Χ2: 1 / Net I/σ(I): 8.2 |
| Reflection shell | Resolution: 2→2.03 Å / % possible obs: 100 % / Redundancy: 4.5 % / Rmerge(I) obs: 1.256 / Num. measured all: 65499 / Num. unique obs: 14443 / CC1/2: 0.48 / Rpim(I) all: 0.661 / Rrim(I) all: 1.422 / Χ2: 1 / Net I/σ(I) obs: 1.3 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→48.9 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.951 / SU B: 6.81 / SU ML: 0.096 / Cross valid method: THROUGHOUT / ESU R: 0.139 / ESU R Free: 0.122 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 24.3 Å2
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| Refinement step | Cycle: 1 / Resolution: 2→48.9 Å
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| Refine LS restraints |
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About Yorodumi



Flavonifractor plautii (bacteria)
X-RAY DIFFRACTION
Canada, 1items
Citation

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