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- PDB-2ww0: Structure of the Family GH92 Inverting Mannosidase BT3990 from Ba... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ww0 | ||||||
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Title | Structure of the Family GH92 Inverting Mannosidase BT3990 from Bacteroides thetaiotaomicron VPI-5482 | ||||||
![]() | PUTATIVE ALPHA-1,2-MANNOSIDASE | ||||||
![]() | HYDROLASE / GH92 / BT3990 / GLYCOSIDE HYDROLASE FAMILY 92 | ||||||
Function / homology | ![]() peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity / glycoprotein catabolic process / protein quality control for misfolded or incompletely synthesized proteins / carbohydrate binding / carbohydrate metabolic process / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Suits, M.D.L. / Thompson, A. / Zhu, Y. / Gilbert, H.J. / Davies, G.J. | ||||||
![]() | ![]() Title: Mechanistic Insights Into a Ca2+-Dependent Family of A-Mannosidases in a Human Gut Symbiont. Authors: Zhu, Y. / Suits, M.D.L. / Thompson, A. / Chavan, S. / Dinev, Z. / Dumon, C. / Smith, N. / Moremen, K.W. / Xiang, Y. / Siriwardena, A. / Williams, S.J. / Gilbert, H.J. / Davies, G.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 941.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 564.4 KB | Display | ![]() |
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Full document | ![]() | 733.8 KB | Display | |
Data in XML | ![]() | 214.1 KB | Display | |
Data in CIF | ![]() | 288 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2wvxSC ![]() 2wvyC ![]() 2wvzC ![]() 2ww1C ![]() 2ww2C ![]() 2ww3C ![]() 2wzsC ![]() 2wx8 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: TRP / Beg label comp-ID: TRP / End auth comp-ID: SER / End label comp-ID: SER / Refine code: 3 / Auth seq-ID: 22 - 753 / Label seq-ID: 3 - 734
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Components
#1: Protein | Mass: 85690.859 Da / Num. of mol.: 8 / Fragment: RESIDUES 20-755 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: VPI-5482 / Plasmid: PET 21A / Production host: ![]() ![]() #2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-SWA / #4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | Nonpolymer details | 1S-8AB-OCTAHYDRO-INDOLIZIDI | Sequence details | FIRST 19 RESIDUES WERE NOT INCLUDED IN RECOMBINAN | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.2 % / Description: NONE |
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Crystal grow | Details: 20% W/V 6000 PEG, 0.2 M NH4CL, TRIS(HYDROXYMETHYL)AMINOMETHANE (PH 8.0) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 7, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0723 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→65.6 Å / Num. obs: 169366 / % possible obs: 98 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Biso Wilson estimate: 53.4 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.7 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 2.9 / % possible all: 95.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2WVX Resolution: 2.8→218.23 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.928 / SU B: 30.595 / SU ML: 0.256 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.333 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY.
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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: 12.646 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→218.23 Å
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Refine LS restraints |
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