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Open data
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Basic information
Entry | Database: PDB / ID: 4oxb | ||||||
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Title | Structure of ECP with sulphate anions at 1.50 Angstroms | ||||||
![]() | Eosinophil cationic protein | ||||||
![]() | HYDROLASE / RNase 3 / Eosinophil Cationic Protein (ECP) | ||||||
Function / homology | ![]() induction of bacterial agglutination / Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA catabolic process / Antimicrobial peptides / RNA nuclease activity / innate immune response in mucosa / lipopolysaccharide binding / chemotaxis / azurophil granule lumen / antimicrobial humoral immune response mediated by antimicrobial peptide ...induction of bacterial agglutination / Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA catabolic process / Antimicrobial peptides / RNA nuclease activity / innate immune response in mucosa / lipopolysaccharide binding / chemotaxis / azurophil granule lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / antibacterial humoral response / endonuclease activity / defense response to Gram-negative bacterium / nucleic acid binding / defense response to Gram-positive bacterium / innate immune response / Neutrophil degranulation / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Blanco, J.A. / Boix, E. / Moussaoui, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of ECP at 1.50 with sulphate anions at 1.50 Angstroms Authors: Blanco, J.A. / Boix, E. / Moussaoui, M. #1: ![]() Title: The sulfate-binding site structure of the human eosinophil cationic protein as revealed by a new crystal form. Authors: Boix, E. / Pulido, D. / Moussaoui, M. / Nogues, M.V. / Russi, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 81.1 KB | Display | ![]() |
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PDB format | ![]() | 61.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 15730.072 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P12724, Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.21 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: Protein resuspended in 20mM sodium cacodylate buffer, pH5.0. 1 uL of protein sample mixed with 1 uL of crystallisation buffer (0.2M lithium sulphate, 0.1M TRIS-HCl pH8.5, 15% PEG4000). PH range: 5.0 - 8.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 10, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→44.12 Å / Num. obs: 38779 / % possible obs: 99.3 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.099 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 1.5→1.58 Å / Rmerge(I) obs: 0.497 / Mean I/σ(I) obs: 2.4 / % possible all: 99.3 |
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Processing
Software | Name: PHENIX / Version: (phenix.refine: 1.8.4_1496) / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.5→44.105 Å / SU ML: 0.18 / σ(F): 1.34 / Phase error: 23.8 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→44.105 Å
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Refine LS restraints |
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LS refinement shell |
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