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- PDB-1slb: X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (G... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1slb | |||||||||
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Title | X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES | |||||||||
![]() | BOVINE GALECTIN-1 | |||||||||
![]() | COMPLEX(LECTIN/SACCHARIDE) / COMPLEX(LECTIN-SACCHARIDE) / COMPLEX(LECTIN-SACCHARIDE) complex | |||||||||
Function / homology | ![]() Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / lactose binding / laminin binding / apoptotic process / extracellular space / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Bourne, Y. / Cambillau, C. | |||||||||
![]() | ![]() Title: Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Authors: Bourne, Y. / Bolgiano, B. / Liao, D.I. / Strecker, G. / Cantau, P. / Herzberg, O. / Feizi, T. / Cambillau, C. #1: ![]() Title: Crystallization and Preliminary X-Ray Diffraction Studies of the Soluble 14kDa Beta-Galactoside-Binding Lectin from Bovine Heart Authors: Bourne, Y. / Bolgiano, B. / Nesa, M.-P. / Penfold, P. / Feizi, T. / Cambillau, C. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.3 KB | Display | ![]() |
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PDB format | ![]() | 99.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 577.4 KB | Display | ![]() |
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Full document | ![]() | 590.5 KB | Display | |
Data in XML | ![]() | 13.7 KB | Display | |
Data in CIF | ![]() | 23.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | GALECTIN-1 MOLECULE EXISTS AS A DIMER. IN THE MONOCLINIC FORM, THERE ARE TWO DIMERS PRESENT IN THE ASYMMETRIC UNIT. EACH MONOMER CONSISTS OF 134 AMINO ACID RESIDUES, ASSIGNED CHAIN IDENTIFIERS A, B, C, AND D. THE TWO MONOMERS ARE RELATED BY A NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS. ONE OLIGOSACCHARIDE UNIT IS PRESENTED PER DIMER. |
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Components
#1: Protein | Mass: 14627.510 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Polysaccharide | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose- ...beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #3: Polysaccharide | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose- ...beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose | Source method: isolated from a genetically manipulated source #4: Water | ChemComp-HOH / | Nonpolymer details | THE N-ACETYLLACTOSAMINE UNIT LOCATED AT THE EXTREMITY OF EACH ANTENNA BINDS TO A DIFFERENT MONOMER ...THE N-ACETYLLACT | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.74 % |
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Crystal grow | *PLUS pH: 5.5 / Method: unknown |
Components of the solutions | *PLUS Conc.: 20-25 % / Common name: PEG |
-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 21316 / % possible obs: 90 % / Observed criterion σ(F): 2 / Num. measured all: 59848 / Rmerge(I) obs: 0.11 |
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Processing
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Refinement | Resolution: 2.3→6 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.177 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.4 |