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Open data
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Basic information
Entry | Database: PDB / ID: 1fcg | ||||||
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Title | ECTODOMAIN OF HUMAN FC GAMMA RECEPTOR, FCGRIIA | ||||||
![]() | PROTEIN (FC RECEPTOR FC(GAMMA)RIIA) | ||||||
![]() | IMMUNE SYSTEM / MEMBRANE PROTEIN / FC RECEPTOR / IMMUNOGLOULIN / LEUKOCYTE / CD32 | ||||||
Function / homology | ![]() IgG receptor activity / antibody-dependent cellular cytotoxicity / IgG binding / FCGR activation / Role of phospholipids in phagocytosis / positive regulation of phagocytosis / FCGR3A-mediated IL10 synthesis / secretory granule membrane / Regulation of actin dynamics for phagocytic cup formation / positive regulation of tumor necrosis factor production ...IgG receptor activity / antibody-dependent cellular cytotoxicity / IgG binding / FCGR activation / Role of phospholipids in phagocytosis / positive regulation of phagocytosis / FCGR3A-mediated IL10 synthesis / secretory granule membrane / Regulation of actin dynamics for phagocytic cup formation / positive regulation of tumor necrosis factor production / cell surface receptor signaling pathway / external side of plasma membrane / Neutrophil degranulation / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Maxwell, K.F. / Powell, M.S. / Garrett, T.P. / Hogarth, P.M. | ||||||
![]() | ![]() Title: Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa. Authors: Maxwell, K.F. / Powell, M.S. / Hulett, M.D. / Barton, P.A. / McKenzie, I.F. / Garrett, T.P. / Hogarth, P.M. #1: ![]() Title: Biochemical Analysis and Crystallisation of Fc(Gamma)RIIA, the Low Affinity Receptor for IgG Authors: Powell, M.S. / Barton, P.A. / Emmanouilidis, D. / Wines, B.D. / Neumann, G.M. / Peitersz, G.A. / Maxwell, K.F. / Garrett, T.P. / Hogarth, P.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 | ![]() | 48.9 KB | Display | ![]() |
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PDB format | ![]() | 35.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.3 KB | Display | ![]() |
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Full document | ![]() | 363.7 KB | Display | |
Data in XML | ![]() | 5.2 KB | Display | |
Data in CIF | ![]() | 7.7 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 19556.863 Da / Num. of mol.: 1 / Fragment: EXTRACELLULAR DOMAINS / Mutation: S88F, R134H Source method: isolated from a genetically manipulated source Details: LOW RESPONDER VARIANT OF FC(GAMMA)RIIA / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 53 % | |||||||||||||||||||||||||
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Crystal grow | pH: 5.6 Details: HANGING DROP VAPOUR DIFFUSION WITH EQUAL VOLUMES OF FC(GAMMA)RIIA AT 6 MG/ML AND MOTHER LIQUOR (0.2 M AMMONIUM ACETATE, 30% W/V PEG 4000, 0.1 M SODIUM CITRATE PH 5.6) MIXED IN 3 MICRO L ...Details: HANGING DROP VAPOUR DIFFUSION WITH EQUAL VOLUMES OF FC(GAMMA)RIIA AT 6 MG/ML AND MOTHER LIQUOR (0.2 M AMMONIUM ACETATE, 30% W/V PEG 4000, 0.1 M SODIUM CITRATE PH 5.6) MIXED IN 3 MICRO L DROPLETS AND ALLOWED TO EQUILIBRATE AT 22 C FOR 3-9 DAYS. | |||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / Method: vapor diffusion, hanging drop / Details: Powell, M.S., (1999) Immunol.Lett., 68, 17. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 108 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Apr 1, 1998 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→10 Å / Num. obs: 15024 / % possible obs: 94.9 % / Redundancy: 2.73 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.53 % / Rmerge(I) obs: 0.359 / Mean I/σ(I) obs: 1.5 / % possible all: 95.9 |
Reflection shell | *PLUS Highest resolution: 2 Å / % possible obs: 95.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Details: NO ELECTRON DENSITY WAS OBSERVED FOR AMINO ACIDS 1-3 OR EITHER OF THE N-LINKED CARBOHYDRATE MOIETIES SO THESE RESIDUES HAVE NOT BEEN MODELLED. MASS SPECTROMETRY INDICATES THAT THESE RESIDUES ...Details: NO ELECTRON DENSITY WAS OBSERVED FOR AMINO ACIDS 1-3 OR EITHER OF THE N-LINKED CARBOHYDRATE MOIETIES SO THESE RESIDUES HAVE NOT BEEN MODELLED. MASS SPECTROMETRY INDICATES THAT THESE RESIDUES ARE PRESENT IN THE CRYSTAL.
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Displacement parameters | Biso mean: 25.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / σ(F): 0 / % reflection Rfree: 8 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 25.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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