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- PDB-1con: THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1con | ||||||
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Title | THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION | ||||||
![]() | CONCANAVALIN A | ||||||
![]() | LECTIN(AGGLUTININ) | ||||||
Function / homology | ![]() regulation of defense response to virus / D-mannose binding / defense response / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Naismith, J.H. / Habash, J. / Harrop, S.J. / Helliwell, J.R. / Hunter, W.N. / Kalb(Gilboa), A.J. / Yariv, J. / Wan, T.C.M. / Weisgerber, S. | ||||||
![]() | ![]() Title: Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution. Authors: Naismith, J.H. / Habash, J. / Harrop, S. / Helliwell, J.R. / Hunter, W.N. / Wan, T.C. / Weisgerber, S. / Kalb, A.J. / Yariv, J. #1: ![]() Title: Non-Glycosylated Recombinant Pro-Concanavalin a is Active without Polypeptide Cleavage Authors: Min, W. / Dunn, A.J. / Jones, D.H. | ||||||
History |
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Remark 700 | SHEET THE MOST STRIKING FEATURE OF CONCANAVALIN A IS TWO LARGE BETA SHEETS IN THE STRUCTURE ...SHEET THE MOST STRIKING FEATURE OF CONCANAVALIN A IS TWO LARGE BETA SHEETS IN THE STRUCTURE COMPRISING 111 OF THE 237 AMINO ACIDS. THERE IS NO ALPHA HELIX. THE REMAINING AMINO ACIDS FORM A SERIES OF LOOPS AND TURNS. THE PURPOSE OF THIS STUDY IS TO PROVIDE A WELL-REFINED SACCHARIDE-FREE STRUCTURE BASED UPON THE CORRECTED AMINO ACID SEQUENCE. THIS STRUCTURE IS PART OF A BROADER STUDY TO DEFINE THE PROTEIN SACCHARIDE INTERACTIONS OF CONCANAVALIN A. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.6 KB | Display | ![]() |
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PDB format | ![]() | 45 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: ALA A 207 - ASP A 208 OMEGA = 0.16 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: THE FOLLOWING SURFACE LOOPS ARE IN WEAK DENSITY: A 118 - A 123, A 149 - A 152, AND A 159 - A 162. | ||||||||
Components on special symmetry positions |
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Components
#1: Protein | Mass: 25622.385 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-CA / | #4: Water | ChemComp-HOH / | Sequence details | THE AUTHORS STATE THAT THIS IS THE CORRECT AMINO ACID SEQUENCE FOR CONCANAVALIN A, ACCORDING TO THE ...THE AUTHORS STATE THAT THIS IS THE CORRECT AMINO ACID SEQUENCE FOR CONCANAVAL | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.4 % |
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Crystal grow | *PLUS Method: other / Details: Kalb, A.J., (1988) J. Crystal Growth, 88, 537. |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 8 Å / Num. obs: 16178 / % possible obs: 99.1 % / Rmerge(I) obs: 0.06 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.1 Å / Num. unique obs: 2188 / Rmerge(I) obs: 0.113 |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 8 Å / Num. reflection all: 16178 / σ(F): 0 / Rfactor all: 0.171 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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