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Yorodumi- PDB-1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bsi | |||||||||
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Title | HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN | |||||||||
Components | ALPHA-AMYLASE | |||||||||
Keywords | HYDROLASE / AMYLASE / PICHIA PASTORIS / GLYCOSYLATED PROTEIN / MUTAGENESIS / DIABETES / CATALYSIS / PANCREATIC / ENZYME / HUMAN | |||||||||
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 | Rydberg, E.H. / Sidhu, G. / Vo, H.C. / Hewitt, J. / Cote, H.C.F. / Wang, Y. / Numao, S. / Macgillivray, R.T.A. / Overall, C.M. / Brayer, G.D. / Withers, S.G. | |||||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Authors: Rydberg, E.H. / Sidhu, G. / Vo, H.C. / Hewitt, J. / Cote, H.C. / Wang, Y. / Numao, S. / MacGillivray, R.T. / Overall, C.M. / Brayer, G.D. / Withers, S.G. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bsi.cif.gz | 110.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bsi.ent.gz | 87.3 KB | Display | PDB format |
PDBx/mmJSON format | 1bsi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bs/1bsi ftp://data.pdbj.org/pub/pdb/validation_reports/bs/1bsi | 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: 55931.305 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: PANCREAS / Production host: Pichia pastoris (fungus) / References: UniProt: P04746, alpha-amylase |
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#2: Sugar | ChemComp-NAG / |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-CL / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.69 % | ||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 33646 / % possible obs: 95.4 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.075 |
Reflection | *PLUS Redundancy: 5 % / Num. measured all: 166575 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.07 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.184 / Mean I/σ(I) obs: 5.8 |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→10 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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LS refinement shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.07 Å |