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Open data
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Basic information
Entry | Database: PDB / ID: 1d9k | |||||||||
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Title | CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA | |||||||||
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![]() | IMMUNE SYSTEM / T-CELL RECEPTOR / MHC CLASS II / D10 / I-AK | |||||||||
Function / homology | ![]() extracellular sequestering of iron ion / organomineral extracellular matrix / Phosphorylation of CD3 and TCR zeta chains / Translocation of ZAP-70 to Immunological synapse / PD-1 signaling / Generation of second messenger molecules / Downstream TCR signaling / antigen processing and presentation of peptide antigen / MHC class II antigen presentation / antimicrobial humoral response ...extracellular sequestering of iron ion / organomineral extracellular matrix / Phosphorylation of CD3 and TCR zeta chains / Translocation of ZAP-70 to Immunological synapse / PD-1 signaling / Generation of second messenger molecules / Downstream TCR signaling / antigen processing and presentation of peptide antigen / MHC class II antigen presentation / antimicrobial humoral response / positive regulation of T cell differentiation / T cell receptor complex / antigen processing and presentation / intracellular sequestering of iron ion / negative regulation of T cell proliferation / multivesicular body / ferric iron binding / acute-phase response / recycling endosome / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / positive regulation of T cell activation / MHC class II protein complex binding / late endosome membrane / iron ion transport / antibacterial humoral response / adaptive immune response / response to lipopolysaccharide / cell surface receptor signaling pathway / lysosome / early endosome / response to xenobiotic stimulus / iron ion binding / immune response / lysosomal membrane / external side of plasma membrane / protein-containing complex binding / Golgi apparatus / cell surface / extracellular space / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Reinherz, E.L. / Tan, K. / Tang, L. / Kern, P. / Liu, J.-H. / Xiong, Y. / Hussey, R.E. / Smolyar, A. / Hare, B. / Zhang, R. ...Reinherz, E.L. / Tan, K. / Tang, L. / Kern, P. / Liu, J.-H. / Xiong, Y. / Hussey, R.E. / Smolyar, A. / Hare, B. / Zhang, R. / Joachimiak, A. / Chang, H.-C. / Wagner, G. / Wang, J.-H. | |||||||||
![]() | ![]() Title: The crystal structure of a T cell receptor in complex with peptide and MHC class II. Authors: Reinherz, E.L. / Tan, K. / Tang, L. / Kern, P. / Liu, J. / Xiong, Y. / Hussey, R.E. / Smolyar, A. / Hare, B. / Zhang, R. / Joachimiak, A. / Chang, H.C. / Wagner, G. / Wang, J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 256.3 KB | Display | ![]() |
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PDB format | ![]() | 205.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 57 KB | Display | |
Data in CIF | ![]() | 77 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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5 | ![]()
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6 | ![]()
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Unit cell |
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Components
-T-CELL RECEPTOR D10 ... , 2 types, 4 molecules AEBF
#1: Protein | Mass: 12399.891 Da / Num. of mol.: 2 / Mutation: C115S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 12131.363 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Protein , 2 types, 4 molecules CGDH
#3: Protein | Mass: 20971.410 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Protein | Mass: 22340.125 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Protein/peptide , 1 types, 2 molecules PQ
#5: Protein/peptide | Mass: 1700.766 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Sugars , 2 types, 6 molecules ![](data/chem/img/NAG.gif)
#6: Polysaccharide | 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #7: Sugar | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.92 Å3/Da / Density % sol: 79.22 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 8000, sodium chloride, TRIS, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 78 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: APS-1 / Detector: CCD / Date: Apr 12, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.069 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→30 Å / Num. all: 501406 / Num. obs: 52056 / % possible obs: 95.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 61.4 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 10 |
Reflection shell | Resolution: 3.2→3.31 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.292 / Mean I/σ(I) obs: 2.26 / % possible all: 87.1 |
Reflection | *PLUS Num. measured all: 501406 / Rmerge(I) obs: 0.07 |
Reflection shell | *PLUS Highest resolution: 3.2 Å / % possible obs: 87.1 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: I-Ak/CA Resolution: 3.2→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh&Huber / Details: Used weighted full matrix least squares procedure
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Displacement parameters | Biso mean: 62.6 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.2→3.34 Å / Total num. of bins used: 8
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3.2 Å / Lowest resolution: 15 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.247 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 62.6 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 3.2 Å / Rfactor Rfree: 0.42 / % reflection Rfree: 10 % / Rfactor Rwork: 0.38 |