+Open data
-Basic information
Entry | Database: PDB / ID: 7taa | ||||||
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Title | FAMILY 13 ALPHA AMYLASE IN COMPLEX WITH ACARBOSE | ||||||
Components | TAKA AMYLASE | ||||||
Keywords | HYDROLASE / GLYCOSYL HYDROLASE / TAKA / AMYLASE / ACARBOSE | ||||||
Function / homology | Function and homology information cell wall-bounded periplasmic space / hyphal septin band / spitzenkorper / fungal-type cell wall / alpha-amylase / cell septum / carbohydrate catabolic process / alpha-amylase activity / calcium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Aspergillus oryzae (mold) | ||||||
Method | X-RAY DIFFRACTION / NATIVE STRUCTURE / Resolution: 1.98 Å | ||||||
Authors | Davies, G.J. / Brzozowski, A.M. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution. Authors: Brzozowski, A.M. / Davies, G.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7taa.cif.gz | 111.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7taa.ent.gz | 91 KB | Display | PDB format |
PDBx/mmJSON format | 7taa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7taa_validation.pdf.gz | 774.3 KB | Display | wwPDB validaton report |
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Full document | 7taa_full_validation.pdf.gz | 782.7 KB | Display | |
Data in XML | 7taa_validation.xml.gz | 24.3 KB | Display | |
Data in CIF | 7taa_validation.cif.gz | 36.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ta/7taa ftp://data.pdbj.org/pub/pdb/validation_reports/ta/7taa | 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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-Components
#1: Protein | Mass: 52525.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Aspergillus oryzae (mold) References: UniProt: P10529, UniProt: P0C1B3*PLUS, alpha-amylase |
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#2: Sugar | ChemComp-ABC / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: 18% MM PEG 5000, 5MM CALCIUM CHLORIDE, 0.1M HEPES BUFFER, PH 7.5. METHOD: HANGING DROP VAPOUR DIFFUSION. THE NATIVE CRYSTALS WERE SOAKED FOR 6 HOURS IN STABILIZING SOLUTION CONTAINING 15 MM ...Details: 18% MM PEG 5000, 5MM CALCIUM CHLORIDE, 0.1M HEPES BUFFER, PH 7.5. METHOD: HANGING DROP VAPOUR DIFFUSION. THE NATIVE CRYSTALS WERE SOAKED FOR 6 HOURS IN STABILIZING SOLUTION CONTAINING 15 MM OF ACARBOSE., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: 1995 / Details: LONG MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→20 Å / Num. obs: 63935 / % possible obs: 97 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 1.98→2.09 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.291 / Mean I/σ(I) obs: 5.1 / % possible all: 94.2 |
Reflection | *PLUS Num. obs: 31062 / Num. measured all: 113411 |
Reflection shell | *PLUS % possible obs: 94.2 % |
-Processing
Software |
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Refinement | Method to determine structure: NATIVE STRUCTURE / Resolution: 1.98→20 Å / Cross valid method: FREE R
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Refinement step | Cycle: LAST / Resolution: 1.98→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.98→2.07 Å / Total num. of bins used: 20
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |