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Yorodumi- PDB-1sla: X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (G... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sla | |||||||||
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Title | X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES | |||||||||
Components | BOVINE GALECTIN-1 | |||||||||
Keywords | COMPLEX(LECTIN/SACCHARIDE) / COMPLEX(LECTIN-SACCHARIDE) / COMPLEX(LECTIN-SACCHARIDE) complex | |||||||||
Function / homology | Function and homology information Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / laminin binding / carbohydrate binding / apoptotic process / extracellular space / cytoplasm Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.45 Å | |||||||||
Authors | Bourne, Y. / Cambillau, C. | |||||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1994 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: Journal: J.Mol.Biol. / Year: 1994 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sla.cif.gz | 64.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sla.ent.gz | 52.5 KB | Display | PDB format |
PDBx/mmJSON format | 1sla.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sl/1sla ftp://data.pdbj.org/pub/pdb/validation_reports/sl/1sla | HTTPS FTP |
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-Related structure data
-Links
-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: (0.52389, 0.00263, -0.851), Vector: Details | GALECTIN-1 MOLECULE EXISTS AS A DIMER. IN THE HEXAGONAL FORM, THERE IS ONE DIMER PRESENT IN THE ASYMMETRIC UNIT. EACH MONOMER CONSISTS OF 134 AMINO ACID RESIDUES, ASSIGNED CHAIN IDENTIFIERS A AND B. THE TWO MONOMERS ARE RELATED BY A NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS. ONE OLIGOSACCHARIDE UNIT IS PRESENTED PER DIMER. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. | |
-Components
#1: Protein | Mass: 14627.510 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Tissue: HEART / References: UniProt: P11116 #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: 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: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.36 Å3/Da / Density % sol: 63.35 % |
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Crystal grow | *PLUS Method: unknown / PH range low: 6 / PH range high: 5 |
Components of the solutions | *PLUS Conc.: 15 % / Common name: PEG |
-Data collection
Reflection | *PLUS Highest resolution: 2.45 Å / Num. obs: 14407 / % possible obs: 94 % / Observed criterion σ(F): 2 / Num. measured all: 99000 / Rmerge(I) obs: 0.13 |
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-Processing
Software |
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Refinement | Resolution: 2.45→6 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.45→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.46 |