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Open data
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Basic information
Entry | Database: PDB / ID: 1bhe | ||||||
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Title | POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA | ||||||
![]() | POLYGALACTURONASE | ||||||
![]() | GLYCOSIDASE / FAMILY 28 GLYCOSYL HYDROLASE / HYDROLYSES POLYGALACTURONIC ACID | ||||||
Function / homology | ![]() endo-polygalacturonase / polygalacturonase activity / cell wall organization / carbohydrate metabolic process / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pickersgill, R. / Smith, D. / Worboys, K. / Jenkins, J. | ||||||
![]() | ![]() Title: Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora. Authors: Pickersgill, R. / Smith, D. / Worboys, K. / Jenkins, 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 | ![]() | 83.5 KB | Display | ![]() |
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PDB format | ![]() | 67.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 420.2 KB | Display | ![]() |
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Full document | ![]() | 421.7 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 26.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 40135.223 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Species: Pectobacterium carotovorum / Strain: subsp. carotovorum Description: SEE H. HEMILA, R. PAKKANEN, R. HEIKINHEIMO, E. TAPIO PALVA & I. PALVA (1992) GENE 116, 27-33 Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 42 % | |||||||||||||||||||||||||
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Crystal grow | pH: 6.5 Details: PROTEIN WAS CRYSTALLIZED FROM 18% PEG 8000, 0.1M SODIUM CACODYLATE, PH 6.5, 0.2M MAGNESIUM ACETATE. | |||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.9 Å / Num. obs: 31103 / % possible obs: 97 % / Redundancy: 3 % / Biso Wilson estimate: 13 Å2 / Rmerge(I) obs: 0.038 / Net I/σ(I): 21 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.114 / Mean I/σ(I) obs: 9 / % possible all: 95 |
Reflection shell | *PLUS % possible obs: 95.2 % |
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Processing
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Refinement | Method to determine structure: ![]() Details: THE DENSITY AND STEREOCHEMISTRY FOR ASP 129 ARE POOR.
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Displacement parameters | Biso mean: 16 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→12.5 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.198 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |