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- PDB-5cj8: Human Osteoclast Associated Receptor (OSCAR) extracellular domain -

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Basic information

Entry
Database: PDB / ID: 5cj8
TitleHuman Osteoclast Associated Receptor (OSCAR) extracellular domain
ComponentsOsteoclast-associated immunoglobulin-like receptor
KeywordsIMMUNE 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
Immunoglobulin domain / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Osteoclast-associated immunoglobulin-like receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.015 Å
AuthorsGao, G.F. / Qi, J. / Shi, Y. / Haywood, J.
CitationJournal: 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
DepositionJul 14, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jan 20, 2016Provider: repository / Type: Initial release
Revision 1.1Feb 10, 2016Group: Database references
Revision 1.2Nov 8, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Osteoclast-associated immunoglobulin-like receptor


Theoretical massNumber of molelcules
Total (without water)20,3691
Polymers20,3691
Non-polymers00
Water1,20767
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area10030 Å2
Unit cell
Length a, b, c (Å)27.215, 46.464, 66.980
Angle α, β, γ (deg.)90.00, 93.25, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Osteoclast-associated immunoglobulin-like receptor / hOSCAR / Polymeric immunoglobulin receptor 3 / Poly-Ig receptor 3


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
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 67 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.08 Å3/Da / Density % sol: 40.74 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, sitting drop
Details: 0.2 M potassium fluoride, 20% w/v polyethylene glycol 3,350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 6, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 10875 / % possible obs: 99.8 % / Redundancy: 5.8 % / Net I/σ(I): 20.3

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Processing

SoftwareName: PHENIX / Version: 1.7.3_928 / Classification: refinement
RefinementMethod 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
RfactorNum. reflection% reflection
Rfree0.2554 515 4.74 %
Rwork0.223 --
obs0.2247 10875 97.32 %
Solvent computationShrinkage 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
Baniso -1Baniso -2Baniso -3
1--0.2659 Å2-0 Å22.1303 Å2
2---3.3612 Å2-0 Å2
3---3.6271 Å2
Refinement stepCycle: LAST / Resolution: 2.015→33.436 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1400 0 0 67 1467
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0091456
X-RAY DIFFRACTIONf_angle_d1.3281993
X-RAY DIFFRACTIONf_dihedral_angle_d15.548532
X-RAY DIFFRACTIONf_chiral_restr0.09214
X-RAY DIFFRACTIONf_plane_restr0.007261
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0149-2.21760.34481040.28272376X-RAY DIFFRACTION90
2.2176-2.53840.3491330.29542652X-RAY DIFFRACTION100
2.5384-3.19770.31061230.26452649X-RAY DIFFRACTION100
3.1977-33.44080.2091550.18222683X-RAY DIFFRACTION99
Refinement TLS params.Method: refined / Origin x: 5.4784 Å / Origin y: 1.5404 Å / Origin z: 22.594 Å
111213212223313233
T0.2107 Å20.0021 Å2-0.0194 Å2-0.2686 Å2-0.0088 Å2--0.2451 Å2
L-0.0807 °2-0.1086 °2-0.4849 °2-0.728 °20.3315 °2--0.8866 °2
S0.0226 Å °-0.0183 Å °0.0102 Å °-0.0012 Å °0.0141 Å °-0.0338 Å °0.0921 Å °-0.0195 Å °-0 Å °
Refinement TLS groupSelection details: all

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