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Yorodumi- PDB-5cj8: Human Osteoclast Associated Receptor (OSCAR) extracellular domain -
+Open data
-Basic information
Entry | Database: PDB / ID: 5cj8 | ||||||
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Title | Human Osteoclast Associated Receptor (OSCAR) extracellular domain | ||||||
Components | Osteoclast-associated immunoglobulin-like receptor | ||||||
Keywords | IMMUNE SYSTEM / Immunoglobulin-like / monomer | ||||||
Function / homology | Function and homology information collagen receptor activity / osteoclast differentiation / specific granule lumen / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / tertiary granule lumen / Neutrophil degranulation / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.015 Å | ||||||
Authors | Gao, G.F. / Qi, J. / Shi, Y. / Haywood, J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2016 Title: Structural basis of collagen recognition by human osteoclast-associated receptor and design of osteoclastogenesis inhibitors. Authors: Haywood, J. / Qi, J. / Chen, C.C. / Lu, G. / Liu, Y. / Yan, J. / Shi, Y. / Gao, G.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5cj8.cif.gz | 85.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5cj8.ent.gz | 62.2 KB | Display | PDB format |
PDBx/mmJSON format | 5cj8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cj/5cj8 ftp://data.pdbj.org/pub/pdb/validation_reports/cj/5cj8 | HTTPS FTP |
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-Related structure data
Related structure data | 5cjbC 1b6uS 1g0xS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20369.395 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 31-215 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: OSCAR / Production host: Escherichia coli (E. coli) / References: UniProt: Q8IYS5 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.74 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop Details: 0.2 M potassium fluoride, 20% w/v polyethylene glycol 3,350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 6, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 10875 / % possible obs: 99.8 % / Redundancy: 5.8 % / Net I/σ(I): 20.3 |
-Processing
Software | Name: PHENIX / Version: 1.7.3_928 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1G0X, 1B6U Resolution: 2.015→33.436 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 31.2 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 46.088 Å2 / ksol: 0.363 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.015→33.436 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 5.4784 Å / Origin y: 1.5404 Å / Origin z: 22.594 Å
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Refinement TLS group | Selection details: all |