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Open data
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Basic information
| Entry | Database: PDB / ID: 3fru | ||||||||||||
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| Title | NEONATAL FC RECEPTOR, PH 6.5 | ||||||||||||
Components |
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Keywords | COMPLEX (IMMUNOGLOBULIN/BINDING PROTEIN) / COMPLEX (IMMUNOGLOBULIN-BINDING PROTEIN) / COMPLEX (IMMUNOGLOBULIN-BINDING PROTEIN) complex | ||||||||||||
| Function / homology | Function and homology informationEndosomal/Vacuolar pathway / DAP12 interactions / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / IgG receptor activity / IgG binding / Neutrophil degranulation / beta-2-microglobulin binding ...Endosomal/Vacuolar pathway / DAP12 interactions / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / IgG receptor activity / IgG binding / Neutrophil degranulation / beta-2-microglobulin binding / humoral immune response / response to cadmium ion / cellular response to iron ion / peptide antigen assembly with MHC class II protein complex / cellular response to iron(III) ion / MHC class II protein complex / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / iron ion transport / peptide antigen assembly with MHC class I protein complex / regulation of iron ion transport / regulation of erythrocyte differentiation / HFE-transferrin receptor complex / response to molecule of bacterial origin / MHC class I peptide loading complex / T cell mediated cytotoxicity / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / MHC class I protein complex / positive regulation of T cell activation / peptide antigen binding / positive regulation of receptor-mediated endocytosis / negative regulation of neurogenesis / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / multicellular organismal-level iron ion homeostasis / negative regulation of epithelial cell proliferation / MHC class II protein complex binding / late endosome membrane / sensory perception of smell / positive regulation of cellular senescence / T cell differentiation in thymus / negative regulation of neuron projection development / protein refolding / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / endosome membrane / immune response / response to xenobiotic stimulus / lysosomal membrane / external side of plasma membrane / structural molecule activity / protein homodimerization activity / extracellular space / identical protein binding Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.2 Å | ||||||||||||
Authors | Vaughn, D.E. / Burmeister, W.P. / Bjorkman, P.J. | ||||||||||||
Citation | Journal: Structure / Year: 1998Title: Structural basis of pH-dependent antibody binding by the neonatal Fc receptor. Authors: Vaughn, D.E. / Bjorkman, P.J. #1: Journal: Nature / Year: 1994Title: Crystal Structure at 2.2 A Resolution of the Mhc-Related Neonatal Fc Receptor Authors: Burmeister, W.P. / Gastinel, L.N. / Simister, N.E. / Blum, M.L. / Bjorkman, P.J. | ||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3fru.cif.gz | 250.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3fru.ent.gz | 201.6 KB | Display | PDB format |
| PDBx/mmJSON format | 3fru.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fr/3fru ftp://data.pdbj.org/pub/pdb/validation_reports/fr/3fru | HTTPS FTP |
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-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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| Unit cell |
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| Details | THIS ENTRY CONSISTS OF THREE FCRN HETERODIMERS AS THEY ARE ARRANGED IN THE ASYMMETRIC UNIT. THE HEAVY CHAINS COMPRISE RESIDUES A 1 - A 269, C 1 - C 269, AND E 5 - E 269. WITHIN EACH HEAVY CHAIN THERE ARE THREE DOMAINS: ALPHA1 (1 - 87), ALPHA2 (88 - 179) AND ALPHA3 (179 - 269). THE LIGHT CHAINS ARE B 1 - B 99 (ASSOCIATED WITH HEAVY CHAIN A), D 1 - D 99 (ASSOCIATED WITH HEAVY CHAIN C) AND F 1 - F 99 (ASSOCIATED WITH HEAVY CHAIN E). |
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Components
-Protein , 2 types, 6 molecules ACEBDF
| #1: Protein | Mass: 30322.887 Da / Num. of mol.: 3 / Fragment: EXTRACELLULAR LIGAND BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 11652.282 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 3 types, 4 molecules 
| #3: 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-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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| #4: Polysaccharide | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-2)-alpha-D-mannopyranose- ...beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
| #5: Sugar |
-Non-polymers , 3 types, 625 molecules 




| #6: Chemical | | #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.5 Å3/Da / Density % sol: 66 % | ||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | pH: 6.5 / Details: PH 6.5 | ||||||||||||||||||||||||||||||||||||||||||
| Crystal grow | *PLUS Temperature: 22 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 |
| Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Jan 1, 1992 |
| Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
| Reflection | Resolution: 2.2→25 Å / Num. obs: 83821 / % possible obs: 86 % / Observed criterion σ(I): -3 / Redundancy: 5.2 % / Rmerge(I) obs: 0.072 |
| Reflection | *PLUS Num. measured all: 436000 |
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Processing
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| Refinement | Method to determine structure: MIR / Resolution: 2.2→25 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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| Solvent computation | Solvent model: FLAT / Bsol: 82.37 Å2 / ksol: 0.348 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 51.6 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.2→25 Å
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| Refine LS restraints |
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| Refine LS restraints NCS | NCS model details: RESTRAINED / Rms dev position: 30 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Xplor file |
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| Software | *PLUS Name: 'CNS DEVELOPMENTAL' / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS |
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