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Open data
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Basic information
Entry | Database: PDB / ID: 1tii | ||||||
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Title | ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB | ||||||
![]() | (HEAT LABILE ENTEROTOXIN TYPE IIB) x 3 | ||||||
![]() | ENTEROTOXIN / ADP-RIBOSYL TRANSFERASE / ADP-RIBOSYLATION / GANGLIOSIDE RECEPTOR | ||||||
Function / homology | ![]() perturbation of signal transduction in another organism / : / host cell membrane / toxin activity / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Van Den Akker, F. / Hol, W.G.J. | ||||||
![]() | ![]() Title: Crystal structure of a new heat-labile enterotoxin, LT-IIb. Authors: van den Akker, F. / Sarfaty, S. / Twiddy, E.M. / Connell, T.D. / Holmes, R.K. / Hol, W.G. #1: ![]() Title: Crystal Structure of a Cholera Toxin-Related Heat-Labile Enterotoxin from E. Coli Authors: Sixma, T.K. / Pronk, S.E. / Kalk, K.H. / Wartna, E.S. / Van Zanten, B.A. / Witholt, B. / Hol, W.G. #2: ![]() Title: Cloning, Nucleotide Sequence, and Hybridization Studies of the Type Iib Heat-Labile Enterotoxin Gene of Escherichia Coli Authors: Pickett, C.L. / Twiddy, E.M. / Coker, C. / Holmes, R.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 144.7 KB | Display | ![]() |
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PDB format | ![]() | 120.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 454.4 KB | Display | ![]() |
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Full document | ![]() | 462.8 KB | Display | |
Data in XML | ![]() | 27.8 KB | Display | |
Data in CIF | ![]() | 40.2 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: 10778.190 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Details: LATENT/INACTIVE FORM / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | | Mass: 21334.432 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: LATENT/INACTIVE FORM / Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Protein | | Mass: 5908.632 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: LATENT/INACTIVE FORM / Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Water | ChemComp-HOH / | Compound details | THE ASYMMETRIC UNIT CONTAINS ONE AB5 TOXIN HEXAMER. THE A SUBUNIT CONTAINS TWO FRAGMENTS LINKED BY ...THE ASYMMETRIC | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 60 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 4.7 Details: SITTING DROP VAPOR DIFFUSION RESERVOIR CONTAINS: 2.0M NACL,0.2M LI2SO4, 0.2M NA-ACETATE PH 4.7 AT 4 DEGREES CELSIUS, vapor diffusion - sitting drop, temperature 277K | ||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: IMAGE PLATE / Date: Mar 20, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→100 Å / Num. obs: 44164 / % possible obs: 83 % / Observed criterion σ(I): -3 / Redundancy: 3.5 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 2.25→2.33 Å / Rmerge(I) obs: 0.235 / Mean I/σ(I) obs: 2.56 / % possible all: 68 |
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Processing
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Refinement | Method to determine structure: ![]() Resolution: 2.25→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 30.5 Å2
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Refine analyze | Luzzati coordinate error obs: 0.28 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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