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- PDB-1htl: MUTATION OF A BURIED RESIDUE CAUSES LACK OF ACTIVITY BUT NO CONFO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1htl | ||||||
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Title | MUTATION OF A BURIED RESIDUE CAUSES LACK OF ACTIVITY BUT NO CONFORMATIONAL CHANGE: CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN MUTANT VAL 97--> LYS | ||||||
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![]() | ENTEROTOXIN | ||||||
Function / homology | ![]() toxin activity / killing of cells of another organism / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Merritt, E.A. / Hol, W.G.J. | ||||||
![]() | ![]() Title: Mutation of a buried residue causes loss of activity but no conformational change in the heat-labile enterotoxin of Escherichia coli. Authors: Merritt, E.A. / Sarfaty, S. / Pizza, M. / Domenighini, M. / Rappuoli, R. / Hol, W.G. #1: ![]() Title: Refined Structure of Escherichia Coli Heat-Labile Enterotoxin, a Close Relative of Cholera Toxin Authors: Sixma, T.K. / Kalk, K.H. / Van Zanten, B.A.M. / Dauter, Z. / Kingma, J. / Witholt, B. / Hol, W.G.J. #2: ![]() 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.M. / Witholt, B. / Hol, W.G.J. #3: ![]() Title: Probing the Structure-Activity Relationship of Escherichia Coli Lt-A by Site-Directed Mutagenesis Authors: Pizza, M. / Domenighini, M. / Hol, W. / Giannelli, V. / Fontana, M.R. / Giuliani, M.M. / Magagnoli, C. / Peppoloni, S. / Manetti, R. / Rappuoli, R. | ||||||
History |
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Remark 700 | SHEET IN THE PENTAMER THE BETA SHEETS FROM ADJACENT MONOMERS COMBINE TO FORM A CONTINUOUS SIX- ...SHEET IN THE PENTAMER THE BETA SHEETS FROM ADJACENT MONOMERS COMBINE TO FORM A CONTINUOUS SIX-STRANDED ANTI-PARALLEL SHEET ACROSS EACH MONOMER-MONOMER INTERFACE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 156 KB | Display | ![]() |
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PDB format | ![]() | 125.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Atom site foot note | 1: CIS PROLINE - PRO D 93 / 2: CIS PROLINE - PRO E 93 / 3: CIS PROLINE - PRO F 93 / 4: CIS PROLINE - PRO G 93 / 5: CIS PROLINE - PRO H 93 / 6: CIS PROLINE - PRO A 178 | ||||||||
Details | ASYMMETRIC UNIT CONTAINS ONE AB5 TOXIN HEXAMER. THE A SUBUNIT CONTAINS TWO FRAGMENTS, CONVENTIONALLY REFERRED TO AS A1 AND A2, WHICH ARE LABELED AS CHAINS A AND C IN THIS COORDINATE SET. |
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Components
#1: Protein | Mass: 11807.539 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | | Mass: 21959.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Protein/peptide | | Mass: 5940.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.29 % | |||||||||||||||
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Crystal grow | *PLUS pH: 10.1 / Method: vapor diffusion, sitting drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 19608 / % possible obs: 75 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 2.5 Å / Rmerge(I) obs: 0.113 |
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Processing
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Refinement | Resolution: 2.5→15 Å / σ(F): 1
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Displacement parameters | Biso mean: 21.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→15 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |