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Open data
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Basic information
| Entry | Database: PDB / ID: 8q5u | ||||||
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| Title | Endoglycosidase S2 in complex with IgG1 Fc | ||||||
Components |
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Keywords | IMMUNE SYSTEM / Antibody / IgG / Fc / endoglycosidase S2 / EndoS2 | ||||||
| Function / homology | Function and homology informationmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase / immunoglobulin complex / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate metabolic process / adaptive immune response / extracellular region / metal ion binding / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) Streptococcus pyogenes (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Sudol, A.S.L. / Tews, I. / Crispin, M. | ||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: J.Biol.Chem. / Year: 2024Title: The IgG-specific endoglycosidases EndoS and EndoS2 are distinguished by conformation and antibody recognition. Authors: Sudol, A.S.L. / Crispin, M. / Tews, I. | ||||||
| History |
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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 | 8q5u.cif.gz | 2.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8q5u.ent.gz | 1.6 MB | Display | PDB format |
| PDBx/mmJSON format | 8q5u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q5/8q5u ftp://data.pdbj.org/pub/pdb/validation_reports/q5/8q5u | HTTPS FTP |
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-Related structure data
| 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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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
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Components
-Protein , 2 types, 6 molecules ACBDEF
| #1: Protein | Mass: 25544.967 Da / Num. of mol.: 3 / Mutation: L234C E382A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DKFZp686C11235 / Cell line (production host): Freestyle HEK293-F cells / Production host: Homo sapiens (human) / References: UniProt: Q6MZV7#2: Protein | Mass: 92581.242 Da / Num. of mol.: 3 / Mutation: D184A E186L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus pyogenes (bacteria) / Gene: endoS / Production host: ![]() |
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-Sugars , 2 types, 2 molecules
| #3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Type: oligosaccharide / Mass: 1463.349 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
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| #4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Type: oligosaccharide / Mass: 1260.157 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
-Non-polymers , 4 types, 293 molecules 






| #5: Chemical | ChemComp-GOL / #6: Chemical | ChemComp-PGE / #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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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: 2.98 Å3/Da / Density % sol: 58.78 % |
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: Morpheus (Molecular Dimensions) conditon G12: 0.1 M carboxylic acids(0.2M Sodium formate; 0.2M Ammonium acetate; 0.2M Sodium citrate tribasic dihydrate; 0.2M Potassium sodium tartrate ...Details: Morpheus (Molecular Dimensions) conditon G12: 0.1 M carboxylic acids(0.2M Sodium formate; 0.2M Ammonium acetate; 0.2M Sodium citrate tribasic dihydrate; 0.2M Potassium sodium tartrate tetrahydrate; 0.2M Sodium oxamate); 0.1 M buffer system 3(Tris (base); BICINE); pH 8.5; 37.5 v/v Precipitant Mix 4 (25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350) |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å |
| Detector | Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: May 24, 2023 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
| Reflection | Resolution: 3→49.91 Å / Num. obs: 85926 / % possible obs: 100 % / Redundancy: 27.5 % / Biso Wilson estimate: 77 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.187 / Rpim(I) all: 0.036 / Rrim(I) all: 0.191 / Net I/σ(I): 12.6 |
| Reflection shell | Resolution: 3→3.05 Å / Rmerge(I) obs: 2.614 / Mean I/σ(I) obs: 0.5 / Num. unique obs: 4250 / CC1/2: 0.64 / Rpim(I) all: 0.527 / Rrim(I) all: 2.668 / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→49.91 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.918 / SU B: 46.453 / SU ML: 0.384 / Cross valid method: FREE R-VALUE / ESU R Free: 0.391 Details: Hydrogens have been added in their riding positions
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 100.098 Å2
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| Refinement step | Cycle: LAST / Resolution: 3→49.91 Å
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About Yorodumi




Homo sapiens (human)
Streptococcus pyogenes (bacteria)
X-RAY DIFFRACTION
United Kingdom, 1items
Citation
PDBj

