+Open data
-Basic information
Entry | Database: PDB / ID: 1xgz | |||||||||
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Title | Structure of the N298S variant of human pancreatic alpha-amylase | |||||||||
Components | Alpha-amylase, pancreatic | |||||||||
Keywords | HYDROLASE / Chloride / Amylase / Enzyme / Acarbose / Inhibitor | |||||||||
Function / homology | Function and homology information polysaccharide digestion / Digestion of dietary carbohydrate / alpha-amylase / carbohydrate catabolic process / alpha-amylase activity / chloride ion binding / carbohydrate metabolic process / calcium ion binding / extracellular space / extracellular exosome / extracellular region Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Maurus, R. / Begum, A. / Kuo, H.H. / Racaza, A. / Numao, S. / Overall, C.M. / Withers, S.G. / Brayer, G.D. | |||||||||
Citation | Journal: PROTEIN SCI. / Year: 2005 Title: Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase Authors: Maurus, R. / Begum, A. / Kuo, H.H. / Racaza, A. / Numao, S. / Andersen, C. / Tams, J.W. / Vind, J. / Overall, C.M. / Withers, S.G. / Brayer, G.D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xgz.cif.gz | 119.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xgz.ent.gz | 89.9 KB | Display | PDB format |
PDBx/mmJSON format | 1xgz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xg/1xgz ftp://data.pdbj.org/pub/pdb/validation_reports/xg/1xgz | HTTPS FTP |
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-Related structure data
Related structure data | 1xh0C 1xh1C 1xh2C 1bsiS C: citing same article (ref.) S: Starting model for refinement |
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Similar 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: 55904.281 Da / Num. of mol.: 1 / Mutation: N298S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Pichia pastoris (fungus) / References: UniProt: P04746, alpha-amylase |
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#2: Sugar | ChemComp-NAG / |
#3: Chemical | ChemComp-CA / |
#4: 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: 2.15 Å3/Da / Density % sol: 42.74 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: MPD, cacodylate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 16, 2002 |
Radiation | Monochromator: osmic mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→25 Å / Num. obs: 33697 / % possible obs: 93 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Rmerge(I) obs: 0.055 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1BSI Resolution: 2→10 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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