+Open data
-Basic information
Entry | Database: PDB / ID: 1poo | ||||||
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Title | THERMOSTABLE PHYTASE FROM BACILLUS SP | ||||||
Components | PROTEIN (PHYTASE) | ||||||
Keywords | HYDROLASE / PHYTASEPHYTASE / PHOSPHATASE / THERMOSTABLE / BACILLUS | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacillus amyloliquefaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.1 Å | ||||||
Authors | Oh, B.H. / Ha, N.C. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2000 Title: Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states. Authors: Ha, N.C. / Oh, B.C. / Shin, S. / Kim, H.J. / Oh, T.K. / Kim, Y.O. / Choi, K.Y. / Oh, B.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1poo.cif.gz | 81.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1poo.ent.gz | 60.5 KB | Display | PDB format |
PDBx/mmJSON format | 1poo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1poo_validation.pdf.gz | 414.5 KB | Display | wwPDB validaton report |
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Full document | 1poo_full_validation.pdf.gz | 418.7 KB | Display | |
Data in XML | 1poo_validation.xml.gz | 14.8 KB | Display | |
Data in CIF | 1poo_validation.cif.gz | 19.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/po/1poo ftp://data.pdbj.org/pub/pdb/validation_reports/po/1poo | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 39008.785 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: ASP 258 IS CIS-ASP / Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Strain: DS11 / Cellular location: EXTRACELLULAR / Gene: PHY / Production host: Bacillus subtilis (bacteria) / References: UniProt: O66037, 3-phytase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 4 |
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-Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.3 % | ||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: 20% MPD, 0.1M MES (PH 6.5) | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: Ha, N.C., (1999) Acta Crystallogr., D55, 691. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 296 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6B / Wavelength: 1.5418 |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 20586 / % possible obs: 97.3 % / Observed criterion σ(I): 2 / Redundancy: 2.5 % / Rsym value: 6.1 |
Reflection | *PLUS Rmerge(I) obs: 0.061 |
Reflection shell | *PLUS % possible obs: 94.5 % / Rmerge(I) obs: 0.264 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2.1→8 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |