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- PDB-2qv4: Human pancreatic alpha-amylase complexed with nitrite and acarbose -
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Open data
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Basic information
Entry | Database: PDB / ID: 2qv4 | |||||||||
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Title | Human pancreatic alpha-amylase complexed with nitrite and acarbose | |||||||||
![]() | Pancreatic alpha-amylase | |||||||||
![]() | HYDROLASE / AMYLASE / PICHIA PASTORIS / GLYCOSYLATED PROTEIN / MUTAGENESIS / DIABETES / CATALYSIS / PANCREATIC / ENZYME / HUMAN / ANION ACTIVATION / NITRITE / CHLORIDE / ACARBOSE / TRANSGLYCOSYLATION / 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 | ![]() ![]() | |||||||||
![]() | Williams, L.K. / 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 |
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Remark 999 | SEQUENCE The authors state that the modification to glutamine 1 to form PCA happens in vivo. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 124.1 KB | Display | ![]() |
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PDB format | ![]() | 93.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2qmkC ![]() 3baiC ![]() 3bajC ![]() 3bakC ![]() 3bawC ![]() 3baxC ![]() 3bayC ![]() 1hnyS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 55931.305 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 2 types, 2 molecules ![](data/chem/img/NAG.gif)
![](data/chem/img/QV4.gif)
![](data/chem/img/QV4.gif)
#2: Sugar | ChemComp-NAG / |
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#5: Sugar | ChemComp-QV4 / |
-Non-polymers , 3 types, 413 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/NO2.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NO2.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-CA / |
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#4: Chemical | ChemComp-NO2 / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.77 % |
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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 |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Aug 29, 2004 / 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: 1.97→30 Å / Num. obs: 32323 / % possible obs: 97.6 % / Observed criterion σ(I): 0 / Redundancy: 4.5 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 42.5 |
Reflection shell | Resolution: 1.97→2 Å / Redundancy: 4 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 14 / % possible all: 94.5 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HNY Resolution: 1.97→20.33 Å / σ(F): 0
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Displacement parameters | Biso mean: 21.8723 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.97→20.33 Å
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Refine LS restraints |
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