+Open data
-Basic information
Entry | Database: PDB / ID: 1eut | ||||||
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Title | SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH GALACTOSE | ||||||
Components | SIALIDASE | ||||||
Keywords | HYDROLASE / GLYCOSIDASE | ||||||
Function / homology | Function and homology information ganglioside catabolic process / oligosaccharide catabolic process / exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / exo-alpha-sialidase / intracellular membrane-bounded organelle / extracellular region / membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Micromonospora viridifaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.5 Å | ||||||
Authors | Gaskell, A. / Crennell, S.J. / Taylor, G.L. | ||||||
Citation | Journal: Structure / Year: 1995 Title: The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Authors: Gaskell, A. / Crennell, S. / Taylor, G. #1: Journal: J.Mol.Biol. / Year: 1992 Title: Crystallization and Preliminary Crystallographic Study of Neuraminidase from Micromonospora Viridifaciens Authors: Taylor, G. / Dineley, L. / Glowka, M. / Laver, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eut.cif.gz | 116.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eut.ent.gz | 93.7 KB | Display | PDB format |
PDBx/mmJSON format | 1eut.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1eut_validation.pdf.gz | 367.9 KB | Display | wwPDB validaton report |
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Full document | 1eut_full_validation.pdf.gz | 388.2 KB | Display | |
Data in XML | 1eut_validation.xml.gz | 15.1 KB | Display | |
Data in CIF | 1eut_validation.cif.gz | 22.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eu/1eut ftp://data.pdbj.org/pub/pdb/validation_reports/eu/1eut | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 64649.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: LARGE 68KD FORM / Source: (natural) Micromonospora viridifaciens (bacteria) / References: UniProt: Q02834, exo-alpha-sialidase |
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#2: Chemical | ChemComp-NA / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 52 % |
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Crystal | *PLUS |
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Taylor, G., (1992) J.Mol.Biol., 225, 1135. / PH range low: 5.5 / PH range high: 5 |
Components of the solutions | *PLUS Conc.: 8 % / Common name: PEG3350 |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, Hamburg / Beamline: X11 / Wavelength: 0.993 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.993 Å / Relative weight: 1 |
Reflection | Num. obs: 20112 / % possible obs: 79.2 % / Observed criterion σ(I): 1 / Redundancy: 2.5 % / Rmerge(I) obs: 0.039 |
Reflection | *PLUS Highest resolution: 2.5 Å / Num. measured all: 49584 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.7 Å / % possible obs: 76.8 % / Rmerge(I) obs: 0.092 |
-Processing
Software |
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Refinement | Resolution: 2.5→6 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 20.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→6 Å
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Refine LS restraints |
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Xplor file |
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