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- PDB-1cax: DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECUL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cax | ||||||
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Title | DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT | ||||||
![]() | (CANAVALIN) x 2 | ||||||
![]() | SEED STORAGE PROTEIN | ||||||
Function / homology | ![]() nutrient reservoir activity / protein-containing complex / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ko, T-P. / Ng, J.D. / Day, J. / Greenwood, A. / McPherson, A. | ||||||
![]() | ![]() Title: Determination of three crystal structures of canavalin by molecular replacement. Authors: Ko, T.P. / Ng, J.D. / Greenwood, A. / McPherson, A. #1: ![]() Title: The Three-Dimensional Structure of Canavalin from Jack Bean (Canavalia Ensiformis) Authors: Ko, T-P. / Ng, J.D. / Day, J. / McPherson, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 222.5 KB | Display | ![]() |
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PDB format | ![]() | 179.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 20968.727 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 20641.021 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 55.1 % |
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Crystal grow | *PLUS pH: 6.8 / Method: unknown |
Components of the solutions | *PLUS Conc.: 1.0 %(w/v) / Chemical formula: NaCl |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.6 Å / Num. obs: 37938 / Num. measured all: 140046 / Rmerge(I) obs: 0.0548 |
Reflection shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.8 Å / Num. unique obs: 7058 / Num. measured obs: 18236 / Rmerge(I) obs: 0.1744 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.6→8 Å / σ(I): 3 /
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Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.6 Å / Rfactor obs: 0.175 / Rfactor Rwork: 0.185 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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