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- PDB-3e2h: Structure of the m67 high-affinity mutant of the 2C TCR in comple... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3e2h | ||||||
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Title | Structure of the m67 high-affinity mutant of the 2C TCR in complex with Ld/QL9 | ||||||
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![]() | IMMUNE SYSTEM / TCR / MHC / cross-reactivity / high affinity / Glycoprotein / Immune response / Membrane / MHC I / Phosphoprotein / Transmembrane / Immunoglobulin domain / Receptor | ||||||
Function / homology | ![]() Lysine catabolism / oxoglutarate dehydrogenase (NAD+) activity / Citric acid cycle (TCA cycle) / olfactory bulb mitral cell layer development / oxoglutarate dehydrogenase (succinyl-transferring) / : / succinyl-CoA metabolic process / oxoglutarate dehydrogenase (succinyl-transferring) activity / Glyoxylate metabolism and glycine degradation / tangential migration from the subventricular zone to the olfactory bulb ...Lysine catabolism / oxoglutarate dehydrogenase (NAD+) activity / Citric acid cycle (TCA cycle) / olfactory bulb mitral cell layer development / oxoglutarate dehydrogenase (succinyl-transferring) / : / succinyl-CoA metabolic process / oxoglutarate dehydrogenase (succinyl-transferring) activity / Glyoxylate metabolism and glycine degradation / tangential migration from the subventricular zone to the olfactory bulb / cerebellar cortex development / oxoglutarate dehydrogenase complex / pyramidal neuron development / thalamus development / 2-oxoglutarate metabolic process / striatum development / NADH metabolic process / thiamine pyrophosphate binding / T cell receptor complex / tricarboxylic acid cycle / heat shock protein binding / generation of precursor metabolites and energy / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / mitochondrial membrane / hippocampus development / lumenal side of endoplasmic reticulum membrane / glycolytic process / MHC class I protein complex / defense response / positive regulation of T cell mediated cytotoxicity / phagocytic vesicle membrane / peptide antigen binding / protein-folding chaperone binding / adaptive immune response / cell surface receptor signaling pathway / immune response / external side of plasma membrane / signaling receptor binding / mitochondrion / extracellular space / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Colf, L.A. / Garcia, K.C. | ||||||
![]() | ![]() Title: Distinct CDR3 Conformations in TCRs Determine the Level of Cross-Reactivity for Diverse Antigens, but Not the Docking Orientation Authors: Jones, L.L. / Colf, L.A. / Stone, J.D. / Garcia, K.C. / Kranz, D.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.7 KB | Display | ![]() |
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PDB format | ![]() | 65.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.9 KB | Display | ![]() |
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Full document | ![]() | 454.8 KB | Display | |
Data in XML | ![]() | 18.1 KB | Display | |
Data in CIF | ![]() | 23.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3e3qC ![]() 2oi9S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 20541.621 Da / Num. of mol.: 1 Mutation: F8Y, V12T, P15R, I23T, N30D, A49V, I66V, R97W, K131R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1063.202 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: THIS SEQUENCE OCCURS NATURALLY IN MOUSE / References: UniProt: Q60597*PLUS |
#3: Protein | Mass: 12211.760 Da / Num. of mol.: 1 / Mutation: L43P, W82R, G99L, F100E, A101R, S102P, A103Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#4: Protein | Mass: 11910.015 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.45 Å3/Da / Density % sol: 77.44 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 2M ammonium tartrate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 7, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.8→50 Å / Num. obs: 10227 / % possible obs: 95.4 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.194 / Χ2: 1.095 |
Reflection shell | Resolution: 3.8→3.94 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.366 / Num. unique all: 885 / Χ2: 1.016 / % possible all: 85.7 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2OI9 Resolution: 3.8→50 Å / Occupancy max: 1 / Occupancy min: 1 / σ(F): 0
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Solvent computation | Bsol: 18.359 Å2 | ||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 200 Å2 / Biso mean: 67.796 Å2 / Biso min: 3.32 Å2
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Refinement step | Cycle: LAST / Resolution: 3.8→50 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: CNS_TOPPAR:protein_rep.param |