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Open data
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Basic information
Entry | Database: PDB / ID: 1w6n | ||||||
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Title | X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 | ||||||
![]() | (GALECTIN-1) x 2 | ||||||
![]() | LECTIN / CARBOHYDRATE-BINDING PROTEINS / GALACTOSIDES / GALECTIN | ||||||
Function / homology | ![]() galectin complex / lactose binding / plasma cell differentiation / myoblast differentiation / laminin binding / T cell costimulation / Post-translational protein phosphorylation / cell-cell adhesion / positive regulation of inflammatory response / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) ...galectin complex / lactose binding / plasma cell differentiation / myoblast differentiation / laminin binding / T cell costimulation / Post-translational protein phosphorylation / cell-cell adhesion / positive regulation of inflammatory response / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / collagen-containing extracellular matrix / regulation of apoptotic process / positive regulation of canonical NF-kappaB signal transduction / positive regulation of viral entry into host cell / positive regulation of apoptotic process / endoplasmic reticulum lumen / apoptotic process / RNA binding / extracellular space / extracellular exosome / extracellular region / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lopez-Lucendo, M.I.F. / Solis, D. / Kaltner, H. / Gabius, H.J. / Romero, A. | ||||||
![]() | ![]() Title: Growth-Regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-Site Mutations and Their Impact on the Thermodynamics of Ligand Binding Authors: Lopez-Lucendo, M.I.F. / Solis, D. / Andre, S. / Hirabayashi, J. / Kasai, K. / Kaltner, H. / Gabius, H.J. / Romero, A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 71 KB | Display | ![]() |
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PDB format | ![]() | 51.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1gzwSC ![]() 1w6mC ![]() 1w6oC ![]() 1w6pC ![]() 1w6qC S: Starting model for refinement C: citing same article ( |
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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: (Code: given Matrix: (-0.37601, -0.36302, -0.85255), Vector: Details | FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 | |
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Components
#1: Protein | Mass: 14657.447 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
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#2: Protein | Mass: 14641.447 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
#3: Chemical | ChemComp-SO4 / | ||||||
#4: Chemical | ChemComp-BME / #5: Water | ChemComp-HOH / | Compound details | MAY REGULATE CELL APOPTOSIS AND CELL DIFFERENTIATION. ENGINEERED MUTATION CYS 2 SER AND GLY 65 ASP ...MAY REGULATE CELL APOPTOSIS AND CELL DIFFERENTI | Sequence details | CYS 2 ENGINEERED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.4 % |
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Crystal grow | Method: vapor diffusion, sitting drop / pH: 5.6 Details: CRYSTALS WERE OBTAINED IN SITTING DROPS BY MIXING EQUAL VOLUMES OF THE PROTEIN SOLUTION (10 MG/ML) AND THE PRECIPITATING BUFFER (2M AMMONIUM SULPHATE AND 1% BETA-MERCAPTO ETHANOL, PH 5.6) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9073 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→23.81 Å / Num. obs: 37567 / % possible obs: 99.8 % / Redundancy: 5 % / Biso Wilson estimate: 16.4 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 1.65→1.75 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 2.6 / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1GZW Resolution: 1.65→23.81 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 1297796.43 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 39.8233 Å2 / ksol: 0.373848 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.65→23.81 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.75 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
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Xplor file |
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