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Open data
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Basic information
Entry | Database: PDB / ID: 2xuv | ||||||
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Title | The structure of HdeB | ||||||
![]() | HDEB | ||||||
![]() | UNKNOWN FUNCTION | ||||||
Function / homology | ![]() cellular stress response to acidic pH / response to acidic pH / unfolded protein binding / outer membrane-bounded periplasmic space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Naismith, J.H. / Wang, W. | ||||||
![]() | ![]() Title: Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in Hdeb and May Have a Role in Periplasmic Chaperone Function. Authors: Wang, W. / Rasmussen, T. / Harding, A.J. / Booth, N.A. / Booth, I.R. / Naismith, J.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 134.4 KB | Display | ![]() |
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PDB format | ![]() | 116.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.3 KB | Display | ![]() |
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Full document | ![]() | 473.9 KB | Display | |
Data in XML | ![]() | 16 KB | Display | |
Data in CIF | ![]() | 22.5 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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Unit cell |
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Components
#1: Protein | Mass: 9290.586 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THE PERIPLASMIC LEADER SEQUENCE IS CLEAVED OFF DURING SYNTHESIS. HDEB IS FOUND IN THE PERIPLASM. ...THE PERIPLASMI | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.24 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→33 Å / Num. obs: 58562 / % possible obs: 95.3 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Biso Wilson estimate: 19 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 2.7 |
Reflection shell | Resolution: 1.5→1.54 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.21 / Mean I/σ(I) obs: 2.7 / % possible all: 94.5 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. TYR 64 IN THE A SUBUNIT AND TO SOME EXTENT IN THE B SUBUNIT SHOWS EVIDENCE OF METHYLATION.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.701 Å2
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Refinement step | Cycle: LAST / Resolution: 1.5→32.78 Å
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Refine LS restraints |
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