+Open data
-Basic information
Entry | Database: PDB / ID: 3poi | ||||||
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Title | Crystal structure of MASP-1 CUB2 domain bound to Methylamine | ||||||
Components | Mannan-binding lectin serine protease 1 | ||||||
Keywords | HYDROLASE / CUB domain / Ca2+ binding site / complex with methylamine / complement protein / lectin pathway of complement / MBL / MBP / ficolins / Bloodstream | ||||||
Function / homology | Function and homology information Scavenging by Class A Receptors / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / Initial triggering of complement / complement activation, lectin pathway / complement activation / zymogen activation / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / calcium-dependent protein binding / peptidase activity ...Scavenging by Class A Receptors / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / Initial triggering of complement / complement activation, lectin pathway / complement activation / zymogen activation / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / calcium-dependent protein binding / peptidase activity / serine-type endopeptidase activity / calcium ion binding / protein homodimerization activity / extracellular space Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.701 Å | ||||||
Authors | Gingras, A.R. / Moody, P.C.E. / Wallis, R. | ||||||
Citation | Journal: Structure / Year: 2011 Title: Structural Basis of Mannan-Binding Lectin Recognition by Its Associated Serine Protease MASP-1: Implications for Complement Activation. Authors: Gingras, A.R. / Girija, U.V. / Keeble, A.H. / Panchal, R. / Mitchell, D.A. / Moody, P.C. / Wallis, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3poi.cif.gz | 115.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3poi.ent.gz | 95.4 KB | Display | PDB format |
PDBx/mmJSON format | 3poi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/po/3poi ftp://data.pdbj.org/pub/pdb/validation_reports/po/3poi | HTTPS FTP |
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-Related structure data
Related structure data | 3pobC 3podC 3poeC 3pofC 3pogC 3pojC 3ponC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 13091.511 Da / Num. of mol.: 2 / Fragment: MASP-1 CUB2 domain (UNP Residues 188-301) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Crarf, MASP-1/-3, Masp1, Masp3 / Plasmid: pET28A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q8CHN8, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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-Non-polymers , 5 types, 237 molecules
#2: Chemical | #3: Chemical | ChemComp-NME / | #4: Chemical | #5: Chemical | ChemComp-TRS / | #6: Water | ChemComp-HOH / | |
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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: 3.24 Å3/Da / Density % sol: 62.01 % |
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Crystal grow | Temperature: 279 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 1.5M Lithium sulfate, 100mM Tirs buffer, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 279K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 26, 2010 |
Radiation | Monochromator: multi-layer optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 37446 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.07 % / Rmerge(I) obs: 0.087 / Net I/σ(I): 18.01 |
Reflection shell | Resolution: 1.7→1.8 Å / Redundancy: 5.09 % / Rmerge(I) obs: 0.322 / Mean I/σ(I) obs: 4.84 / Num. unique all: 30612 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.701→44.98 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.962 / SU B: 2.456 / SU ML: 0.037 / Cross valid method: THROUGHOUT / ESU R: 0.075 / ESU R Free: 0.067 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.421 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.701→44.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.701→1.746 Å / Total num. of bins used: 20
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