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Open data
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Basic information
Entry | Database: PDB / ID: 5xmm | ||||||||||||
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Title | FLA-E*01801-167W/S | ||||||||||||
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![]() | IMMUNE SYSTEM / Domestic cats / MHC I / Feline immunodeficiency virus / CTL immunity | ||||||||||||
Function / homology | ![]() antigen processing and presentation of peptide antigen via MHC class I / viral budding via host ESCRT complex / antigen processing and presentation / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / phagocytic vesicle membrane / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response ...antigen processing and presentation of peptide antigen via MHC class I / viral budding via host ESCRT complex / antigen processing and presentation / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / phagocytic vesicle membrane / 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 / viral nucleocapsid / nucleic acid binding / structural constituent of virion / immune response / lysosomal membrane / zinc ion binding / extracellular region Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Liang, R. / Sun, Y. / Wang, J. / Wu, Y. / Zhang, N. / Xia, C. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Major Histocompatibility Complex Class I (FLA-E*01801) Molecular Structure in Domestic Cats Demonstrates Species-Specific Characteristics in Presenting Viral Antigen Peptides Authors: Liang, R. / Sun, Y. / Liu, Y. / Wang, J. / Wu, Y. / Li, Z. / Ma, L. / Zhang, N. / Zhang, L. / Wei, X. / Qu, Z. / Zhang, N. / Xia, C. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 166 KB | Display | ![]() |
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PDB format | ![]() | 130.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5xmfC ![]() 3pwvS 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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Unit cell |
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Components
#1: Protein | Mass: 31848.109 Da / Num. of mol.: 1 / Fragment: UNP residues 25-299 / Mutation: W168S Source method: isolated from a genetically manipulated source Details: This protein is the mutant of FLA-B*n06 and W residue was mutated into S residue Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 11618.078 Da / Num. of mol.: 1 / Fragment: UNP residues 21-118 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Protein/peptide | Mass: 951.037 Da / Num. of mol.: 1 / Fragment: UNP residues 21-118 / Mutation: R1D Source method: isolated from a genetically manipulated source Details: This peptide was mutated by feline immunodeficiency virus' gag protein and the R residue was mutated into D residue Source: (gene. exp.) ![]() ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.67 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: PEG/Ion 2; No.28 (0.2M sodium formate and 20%w/v) polyethylene glycol 3,350), 277 K, pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 29, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97931 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→50 Å / Num. obs: 8745 / % possible obs: 83.8 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.568 / Rsym value: 0.092 / Net I/σ(I): 7.31 |
Reflection shell | Resolution: 2.9→3.06 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.568 / Mean I/σ(I) obs: 7.3 / Rsym value: 0.092 / % possible all: 83.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3PWV Resolution: 2.9→50 Å / Cor.coef. Fo:Fc: 0.89 / Cor.coef. Fo:Fc free: 0.845 / SU B: 34.816 / SU ML: 0.303 / Cross valid method: THROUGHOUT / ESU R Free: 0.47
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.614 Å2
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Refinement step | Cycle: 1 / Resolution: 2.9→50 Å
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Refine LS restraints |
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