+Open data
-Basic information
Entry | Database: PDB / ID: 2j61 | ||||||
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Title | L-ficolin complexed to N-acetylglucosamine (forme C) | ||||||
Components | (FICOLIN-2) x 2 | ||||||
Keywords | LECTIN / GLYCOPROTEIN / FICRINOGEN-LIKE / INNATE IMMUNITY / PATTERN RECOGNITION PROTEIN / COLLAGEN / IMMUNOLOGY / LECTIN- LIKE | ||||||
Function / homology | Function and homology information mannan binding / recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / cell surface pattern recognition receptor signaling pathway / opsonization / complement activation, lectin pathway / carbohydrate derivative binding / collagen trimer ...mannan binding / recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / cell surface pattern recognition receptor signaling pathway / opsonization / complement activation, lectin pathway / carbohydrate derivative binding / collagen trimer / serine-type endopeptidase complex / proteoglycan binding / Initial triggering of complement / antigen binding / calcium-dependent protein binding / collagen-containing extracellular matrix / defense response to Gram-negative bacterium / blood microparticle / defense response to Gram-positive bacterium / external side of plasma membrane / signaling receptor binding / proteolysis / extracellular space / extracellular exosome / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Garlatti, V. / Gaboriaud, C. | ||||||
Citation | Journal: Embo J. / Year: 2007 Title: Structural Insights Into the Innate Immune Recognition Specificities of L- and H-Ficolins. Authors: Garlatti, V. / Belloy, N. / Martin, L. / Lacroix, M. / Matsushita, M. / Endo, Y. / Fujita, T. / Fontecilla-Camps, J.C. / Arlaud, G.J. / Thielens, N.M. / Gaboriaud, C. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2j61.cif.gz | 103.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2j61.ent.gz | 78.6 KB | Display | PDB format |
PDBx/mmJSON format | 2j61.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2j61_validation.pdf.gz | 439.1 KB | Display | wwPDB validaton report |
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Full document | 2j61_full_validation.pdf.gz | 467.8 KB | Display | |
Data in XML | 2j61_validation.xml.gz | 15.3 KB | Display | |
Data in CIF | 2j61_validation.cif.gz | 21.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j6/2j61 ftp://data.pdbj.org/pub/pdb/validation_reports/j6/2j61 | HTTPS FTP |
-Related structure data
Related structure data | 2j0gC 2j0hC 2j0yC 2j1gC 2j2pC 2j3fC 2j3gC 2j3oC 2j3uC 2j5zC 2j60C 2j64C 1jc9S 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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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 24757.332 Da / Num. of mol.: 1 / Fragment: BINDING DOMAIN, RESIDUES 97-313 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: PLASMA / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q15485 | ||||||
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#2: Protein | Mass: 24729.318 Da / Num. of mol.: 1 / Fragment: BINDING DOMAIN, RESIDUES 97-313 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: PLASMA / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q15485 | ||||||
#3: Chemical | #4: Sugar | ChemComp-NAG / | #5: Water | ChemComp-HOH / | Sequence details | DOMAINE C TERMINAL DIFFERENCE BETWEEN UNP SEQUENCE AND THE PROTEIN CRYSTALLIZED BECAUSE IT EXISTS ...DOMAINE C TERMINAL DIFFERENCE | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.16 Å3/Da / Density % sol: 60.8 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.9206 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 4, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9206 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→19.39 Å / Num. obs: 16911 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 6.9 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 24.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1JC9 Resolution: 2.7→15 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.867 / SU B: 16.011 / SU ML: 0.331 / Cross valid method: THROUGHOUT / ESU R: 0.843 / ESU R Free: 0.38 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 56.49 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→15 Å
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Refine LS restraints |
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