+Open data
-Basic information
Entry | Database: PDB / ID: 1fsu | |||||||||
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Title | Crystal Structure of 4-Sulfatase (human) | |||||||||
Components | N-ACETYLGALACTOSAMINE-4-SULFATASE | |||||||||
Keywords | HYDROLASE / SULFATASE / GLYCOSAMINOGLYCAN DEGRADATION / GLYCOPROTEIN / LYSOSOME | |||||||||
Function / homology | Function and homology information N-acetylgalactosamine-4-sulfatase / colon epithelial cell migration / MPS VI - Maroteaux-Lamy syndrome / N-acetylgalactosamine-4-sulfatase activity / Glycosphingolipid metabolism / chondroitin sulfate catabolic process / The activation of arylsulfatases / CS/DS degradation / arylsulfatase activity / neutrophil degranulation ...N-acetylgalactosamine-4-sulfatase / colon epithelial cell migration / MPS VI - Maroteaux-Lamy syndrome / N-acetylgalactosamine-4-sulfatase activity / Glycosphingolipid metabolism / chondroitin sulfate catabolic process / The activation of arylsulfatases / CS/DS degradation / arylsulfatase activity / neutrophil degranulation / regulation of epithelial cell migration / response to methylmercury / response to pH / lysosomal transport / lysosome organization / response to nutrient / rough endoplasmic reticulum / lysosomal lumen / central nervous system development / positive regulation of neuron projection development / autophagy / response to estrogen / azurophil granule lumen / ficolin-1-rich granule lumen / lysosome / endoplasmic reticulum lumen / Neutrophil degranulation / cell surface / Golgi apparatus / mitochondrion / extracellular exosome / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.5 Å | |||||||||
Authors | Bond, C. / Guss, M. | |||||||||
Citation | Journal: Structure / Year: 1997 Title: Structure of a human lysosomal sulfatase. Authors: Bond, C.S. / Clements, P.R. / Ashby, S.J. / Collyer, C.A. / Harrop, S.J. / Hopwood, J.J. / Guss, J.M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fsu.cif.gz | 112.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fsu.ent.gz | 87.9 KB | Display | PDB format |
PDBx/mmJSON format | 1fsu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/1fsu ftp://data.pdbj.org/pub/pdb/validation_reports/fs/1fsu | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 55819.074 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: LYSOSOME / Gene: G4S / Organ: LIVER / Cell line (production host): CHO452 / Cellular location (production host): SECRETED / Organelle (production host): LYSOSOME / Production host: Cricetulus griseus (Chinese hamster) / Variant (production host): K1 References: UniProt: P15848, N-acetylgalactosamine-4-sulfatase | ||||||
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#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-CA / | #4: Chemical | ChemComp-CL / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 61 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.1 Details: HANGING DROPS, 0.2 M MALATE/ 0.1 M ACETATE BUFFERED AT PH 5.1. 12-15 % PEG8000, 20% GLYCEROL., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop / Details: Ashby, S.J., (1995) Acta Cryst. D, 51, 1082. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Sep 1, 1995 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.5 Å / Num. obs: 27332 / % possible obs: 92 % / Observed criterion σ(I): -3 / Redundancy: 7.1 % / Biso Wilson estimate: 7.9 Å2 / Rsym value: 0.089 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 2.9 % / Rsym value: 0.25 / % possible all: 72.9 |
Reflection | *PLUS Num. measured all: 194673 / Rmerge(I) obs: 0.089 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Highest resolution: 2.5 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 23.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.59 Å
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 9999 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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