[English] 日本語
![](img/lk-miru.gif)
- PDB-3bak: N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 3bak | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate | |||||||||
![]() | Pancreatic alpha-amylase | |||||||||
![]() | HYDROLASE / Amylase / Anion Activation / Chloride / Nitrate / Human / Pancreatic / Enzyme / Carbohydrate metabolism / Glycoprotein / Glycosidase / Metal-binding / Pyrrolidone carboxylic acid / Secreted | |||||||||
Function / homology | ![]() 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 | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Fredriksen, J.R. / Maurus, R. / Brayer, G.D. | |||||||||
![]() | ![]() Title: Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity Authors: Maurus, R. / Begum, A. / Williams, L.K. / Fredriksen, J.R. / Zhang, R. / Withers, S.G. / Brayer, G.D. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 117.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 88.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 2qmkC ![]() 2qv4C ![]() 3baiC ![]() 3bajC ![]() 3bawC ![]() 3baxC ![]() 3bayC ![]() 1bsiS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 55904.281 Da / Num. of mol.: 1 / Mutation: N298S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
---|---|
#2: Sugar | ChemComp-NAG / |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-NO3 / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 42.09 % |
---|---|
Crystal grow | Temperature: 300 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 60% 2-methylpentane-2,4-diol, 100 mM cacodylate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Details: mirrors |
Radiation | Monochromator: osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. obs: 37873 / Redundancy: 7.5 % / Rmerge(I) obs: 0.54 / Net I/σ(I): 26.4 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB Entry 1BSI Resolution: 1.9→17.14 Å
| ||||||||||||||||||||
Displacement parameters | Biso mean: 24.107 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→17.14 Å
| ||||||||||||||||||||
Refine LS restraints |
|