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Yorodumi- PDB-2aaa: CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2aaa | ||||||
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Title | CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS | ||||||
Components | ALPHA-AMYLASE | ||||||
Keywords | GLYCOSIDASE | ||||||
Function / homology | Function and homology information alpha-amylase activity => GO:0004556 / alpha-amylase / carbohydrate catabolic process / alpha-amylase activity / calcium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Aspergillus niger (mold) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.12 Å | ||||||
Authors | Brady, L. / Brzozowski, A.M. / Derewenda, Z. / Dodson, E.J. / Dodson, G.G. | ||||||
Citation | Journal: Biochemistry / Year: 1990 Title: Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus. Authors: Boel, E. / Brady, L. / Brzozowski, A.M. / Derewenda, Z. / Dodson, G.G. / Jensen, V.J. / Petersen, S.B. / Swift, H. / Thim, L. / Woldike, H.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2aaa.cif.gz | 118.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2aaa.ent.gz | 83.5 KB | Display | PDB format |
PDBx/mmJSON format | 2aaa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2aaa_validation.pdf.gz | 397.5 KB | Display | wwPDB validaton report |
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Full document | 2aaa_full_validation.pdf.gz | 461 KB | Display | |
Data in XML | 2aaa_validation.xml.gz | 21 KB | Display | |
Data in CIF | 2aaa_validation.cif.gz | 30.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aa/2aaa ftp://data.pdbj.org/pub/pdb/validation_reports/aa/2aaa | HTTPS FTP |
-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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Atom site foot note | 1: RESIDUES PRO 139 AND PRO 341 ARE CIS PROLINES. |
-Components
#1: Protein | Mass: 52965.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus niger (mold) / References: UniProt: P56271, alpha-amylase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.61 % |
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Crystal grow | *PLUS Method: unknown / PH range low: 4 / PH range high: 3 |
Components of the solutions | *PLUS Common name: PEG8000 |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.1 Å / Rmerge(I) obs: 0.195 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Resolution: 2.12→7 Å / Rfactor obs: 0.169 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.12→7 Å
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Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 7 Å / Rfactor obs: 0.169 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |