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Yorodumi- PDB-1hng: CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM O... -
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-Basic information
Entry | Database: PDB / ID: 1hng | ||||||
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Title | CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2 | ||||||
Components | CD2 | ||||||
Keywords | T LYMPHOCYTE ADHESION GLYCOPROTEIN | ||||||
Function / homology | Function and homology information natural killer cell mediated cytotoxicity / natural killer cell activation / heterotypic cell-cell adhesion / positive regulation of interleukin-8 production / cytoplasmic side of plasma membrane / cell-cell adhesion / receptor tyrosine kinase binding / : / cell-cell junction / positive regulation of type II interferon production ...natural killer cell mediated cytotoxicity / natural killer cell activation / heterotypic cell-cell adhesion / positive regulation of interleukin-8 production / cytoplasmic side of plasma membrane / cell-cell adhesion / receptor tyrosine kinase binding / : / cell-cell junction / positive regulation of type II interferon production / positive regulation of tumor necrosis factor production / external side of plasma membrane / signaling receptor binding / protein kinase binding / Golgi apparatus / cell surface / protein-containing complex / extracellular region / nucleoplasm / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Rattus rattus (black rat) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Jones, E.Y. / Davis, S.J. / Williams, A.F. / Harlos, K. / Stuart, D.I. | ||||||
Citation | Journal: Nature / Year: 1992 Title: Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Authors: Jones, E.Y. / Davis, S.J. / Williams, A.F. / Harlos, K. / Stuart, D.I. #1: Journal: To be Published Title: Ligand Binding by the Immunoglobulin Superfamily Recognition Molecule Cd2 is Glycosylation Independent Authors: Davis, S.J. / Davies, E.A. / Barclay, A.N. / Daenke, S. / Bodian, D.L. / Jones, E.Y. / Stuart, D.I. / Butters, T.D. / Dwek, R.A. / Van Der Merwe, P.A. #2: Journal: Protein Eng. / Year: 1993 Title: Expression of Soluble Recombinant Glycoproteins with Predefined Glycosylation: Application to the Crystallization of the T-Cell Glycoprotein Cd2 Authors: Davis, S.J. / Puklavec, M.J. / Ashford, D.A. / Harlos, K. / Jones, E.Y. / Stuart, D.I. / Williams, A.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hng.cif.gz | 74.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hng.ent.gz | 61.6 KB | Display | PDB format |
PDBx/mmJSON format | 1hng.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hn/1hng ftp://data.pdbj.org/pub/pdb/validation_reports/hn/1hng | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20138.020 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus rattus (black rat) / Organ: OVARY / References: UniProt: P08921 Nonpolymer details | FOUR NAG (N-ACETYL GLUCOSAMIN | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.35 Å3/Da / Density % sol: 63.24 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.4 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 13432 / % possible obs: 96 % |
Reflection | *PLUS Num. measured all: 51452 / Rmerge(I) obs: 0.126 |
-Processing
Software |
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Refinement | Resolution: 2.8→20 Å /
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Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||
Refinement | *PLUS Rfactor obs: 0.215 / Rfactor Rwork: 0.215 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: x_bond_d / Dev ideal: 0.015 |