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Open data
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Basic information
Entry | Database: PDB / ID: 1cvn | |||||||||
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Title | CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE | |||||||||
![]() | CONCANAVALIN A | |||||||||
![]() | LECTIN (AGGLUTININ) / CONCANAVALIN A / SACCHARIDE BINDING | |||||||||
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. | |||||||||
![]() | ![]() Title: Structural basis of trimannoside recognition by concanavalin A. Authors: Naismith, J.H. / Field, R.A. #1: ![]() Title: Refined Structure of Concanavalin a Complexed with Methyl Alpha-D-Mannopyranoside at 2.0A Resolution and Comparison with the Saccharide-Free Structure Authors: Naismith, J.H. / Emmerich, C. / Habash, J. / Harrop, S.J. / Helliwell, J.R. / Hunter, W.N. / Raftery, J. / Kalb(Gilboa), A.J. / Yariv, J. #2: ![]() Title: Refined Structure of Cadmium-Substituted Concanavalin a at 2.0A Resolution Authors: Naismith, J.H. / Habash, J. / Harrop, S.J. / Helliwell, J.R. / Hunter, W.N. / Wan, T.C.M. / Weisgerber, S. / Kalb(Gilboa), A.J. / Yariv, J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 199.2 KB | Display | ![]() |
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PDB format | ![]() | 158.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 37.9 KB | Display | |
Data in CIF | ![]() | 52.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5cnaS S: Starting model for refinement |
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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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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 25622.385 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Details: TRIMANNOSIDE COMPLEX / Source: (natural) ![]() ![]() #2: Polysaccharide | alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-MN / #4: Chemical | ChemComp-CA / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||
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Crystal grow | pH: 9 / Details: pH 9.0 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Jul 13, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→8 Å / Num. obs: 48025 / % possible obs: 95.54 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rmerge(I) obs: 0.085 |
Reflection shell | Resolution: 2.3→2.4 Å / Rmerge(I) obs: 0.222 / % possible all: 80 |
Reflection shell | *PLUS % possible obs: 80 % / Redundancy: 1.5 % / Num. unique obs: 5025 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5CNA Resolution: 2.3→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 17.96 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.205 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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