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Open data
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Basic information
Entry | Database: PDB / ID: 1smd | |||||||||
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Title | HUMAN SALIVARY AMYLASE | |||||||||
![]() | AMYLASE | |||||||||
![]() | HYDROLASE (O-GLYCOSYL) / HYDROLASE / O-GLYCOSYL / CARBOHYDRATE METABOLISM | |||||||||
Function / homology | ![]() Digestion of dietary carbohydrate / oligosaccharide metabolic process / alpha-amylase / alpha-amylase activity / chloride ion binding / carbohydrate metabolic process / calcium ion binding / extracellular space / extracellular exosome Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Ramasubbu, N. | |||||||||
![]() | ![]() Title: Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity. Authors: Ramasubbu, N. / Paloth, V. / Luo, Y. / Brayer, G.D. / Levine, M.J. #1: ![]() Title: Crystallization and Preliminary X-Ray Diffraction Analysis of Human Salivary Alpha-Amylase Authors: Ramasubbu, N. / Bhandary, K.K. / Scannapieco, F.A. / Levine, M.J. #2: ![]() Title: Structural Relationship between the Enzymatic and Streptococcal Binding Sites of Human Salivary Alpha-Amylase Authors: Scannapieco, F.A. / Bhandary, K. / Ramasubbu, N. / Levine, M.J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.9 KB | Display | ![]() |
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PDB format | ![]() | 88 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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
#1: Protein | Mass: 55955.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: HUMAN SALIVARY AMYLASE / Source: (natural) ![]() References: UniProt: P04745, UniProt: P0DTE8*PLUS, alpha-amylase |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-CL / |
#4: Water | ChemComp-HOH / |
Compound details | THIS ENTRY HAS A BLOCKED AMINO TERMINUS REFERRED TO AS PCA - PYRROLIDONE CARBOXYLIC ACID (ALSO ...THIS ENTRY HAS A BLOCKED AMINO TERMINUS REFERRED TO AS PCA - PYRROLIDON |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.74 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 9 / Method: vapor diffusion, hanging dropDetails: Ramasubbu, N., (1991) Proteins: Struct.,Funct., Genet., 11, 230. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 30 Å / % possible obs: 93.4 % / Rmerge(I) obs: 0.076 |
Reflection shell | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 2 Å / % possible obs: 88.1 % |
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Processing
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Refinement | Resolution: 1.6→6 Å
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Refinement step | Cycle: LAST / Resolution: 1.6→6 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.184 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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