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- PDB-5a6a: GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in compl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5a6a | ||||||
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Title | GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT | ||||||
![]() | N-ACETYL-BETA-D-GLUCOSAMINIDASE | ||||||
![]() | HYDROLASE / BETA-HEXOSAMINIDASE / STREPTOCOCCUS PNEUMONIAE / BACTERIAL PROTEINS / CARBOHYDRATE CONFORMATION / CATALYTIC DOMAIN / ENZYME INHIBITORS / HOST-PATHOGEN INTERACTIONS / HYDROGEN BONDING / HYDROLYSIS / MODELS / POLYSACCHARIDES / PROTEIN BINDING / VIRULENCE FACTORS | ||||||
Function / homology | ![]() hexosaminidase activity / beta-N-acetylhexosaminidase activity / N-acetyl-beta-D-galactosaminidase activity / carbohydrate metabolic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cid, M. / Robb, C.S. / Higgins, M.A. / Boraston, A.B. | ||||||
![]() | ![]() Title: A Second beta-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans. Authors: Robb, M. / Robb, C.S. / Higgins, M.A. / Hobbs, J.K. / Paton, J.C. / Boraston, A.B. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 240.3 KB | Display | ![]() |
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PDB format | ![]() | 188.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 478.4 KB | Display | ![]() |
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Full document | ![]() | 486.3 KB | Display | |
Data in XML | ![]() | 41.7 KB | Display | |
Data in CIF | ![]() | 57.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5a69C ![]() 5a6bC ![]() 5a6jC ![]() 5a6kC ![]() 5ac4C ![]() 5ac5C ![]() 2epnS 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: 74181.516 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: C1CH75, UniProt: A0A0H2US73*PLUS, beta-N-acetylhexosaminidase #2: Chemical | ChemComp-EDO / | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.84 Å3/Da / Density % sol: 33.21 % / Description: NONE |
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Crystal grow | pH: 10.2 Details: 12% (W/V) PEG 3350, 0.2 M MAGNESIUM CHLORIDE, 0.05 M CAPS, PH 10.2, 1%GLYCEROL |
-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97926 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→40 Å / Num. obs: 28812 / % possible obs: 95.4 % / Observed criterion σ(I): 2 / Redundancy: 7.9 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 24.5 |
Reflection shell | Resolution: 2.7→2.75 Å / Redundancy: 8.3 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 5.2 / % possible all: 94.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2EPN Resolution: 2.69→45.74 Å / Cor.coef. Fo:Fc: 0.916 / Cor.coef. Fo:Fc free: 0.859 / SU B: 15.691 / SU ML: 0.329 / Cross valid method: THROUGHOUT / ESU R Free: 0.458 / 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: 37.689 Å2
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Refinement step | Cycle: LAST / Resolution: 2.69→45.74 Å
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Refine LS restraints |
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