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Open data
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Basic information
Entry | Database: PDB / ID: 2pel | ||||||||||||
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Title | PEANUT LECTIN | ||||||||||||
![]() | PEANUT LECTIN | ||||||||||||
![]() | LECTIN (AGGLUTININ) / LEGUME LECTIN / OPEN QUATERNARY STRUCTURE / CARBOHYDRATE SPECIFICITY / PROTEIN CRYSTALLOGRAPHY / AGGLUTININ | ||||||||||||
Function / homology | ![]() | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() | ||||||||||||
![]() | Banerjee, R. / Das, K. / Ravishankar, R. / Suguna, K. / Surolia, A. / Vijayan, M. | ||||||||||||
![]() | ![]() Title: Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex. Authors: Banerjee, R. / Das, K. / Ravishankar, R. / Suguna, K. / Surolia, A. / Vijayan, M. #1: ![]() Title: Crystal Structure of Peanut Lectin, a Protein with an Unusual Quaternary Structure Authors: Banerjee, R. / Mande, S.C. / Ganesh, V. / Das, K. / Dhanaraj, V. / Mahanta, S.K. / Suguna, K. / Surolia, A. / Vijayan, M. #2: ![]() Title: Preparation and Preliminary X-Ray Studies of Three Acidic Ph Crystal Forms of the Anti-T Lectin from Peanut (Arachis Hypogaea) Authors: Salunke, D.M. / Khan, M.I. / Surolia, A. / Vijayan, M. #3: ![]() Title: Crystallization and Preliminary X-Ray Studies of the Anti-T Lectin from Peanut (Arachis Hypogaea) Authors: Salunke, D.M. / Khan, M.I. / Surolia, A. / Vijayan, M. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 198 KB | Display | ![]() |
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PDB format | ![]() | 157.8 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 | ![]() | 42.3 KB | Display | |
Data in CIF | ![]() | 60.8 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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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 25208.955 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Sugars , 2 types, 4 molecules
#2: Polysaccharide | #3: Polysaccharide | beta-D-galactopyranose-(1-4)-beta-D-glucopyranose / beta-lactose | |
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-Non-polymers , 3 types, 571 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-CA / #5: Chemical | ChemComp-MN / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.13 Å3/Da / Density % sol: 57 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1990 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.25 Å / Num. obs: 50764 / % possible obs: 88 % / Rmerge(I) obs: 0.079 |
Reflection | *PLUS Lowest resolution: 9999 Å / Num. measured all: 173209 |
Reflection shell | *PLUS Highest resolution: 2.25 Å / Lowest resolution: 2.34 Å / % possible obs: 42.3 % / Num. unique obs: 4508 / Num. measured obs: 7107 / Rmerge(I) obs: 0.15 |
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Processing
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Refinement | Resolution: 2.25→10 Å / σ(F): 3 Details: THERE IS A TETRAMER IN THE ASYMMETRIC UNIT WITHOUT 222 OR FOUR-FOLD SYMMETRY.
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Displacement parameters | Biso mean: 22.45 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.12 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.164 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 22.5 Å2 |