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- PDB-7arx: Crystal structure of the catalytic fragment of masp-1 in complex ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7arx | ||||||||||||
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Title | Crystal structure of the catalytic fragment of masp-1 in complex with SFMI1 | ||||||||||||
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![]() | IMMUNE SYSTEM / protease / inhibitor / complex | ||||||||||||
Function / homology | ![]() Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / negative regulation of complement activation / complement activation, lectin pathway / zymogen activation / Scavenging by Class A Receptors / Initial triggering of complement / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / calcium-dependent protein binding / peptidase activity ...Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / negative regulation of complement activation / complement activation, lectin pathway / zymogen activation / Scavenging by Class A Receptors / Initial triggering of complement / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / calcium-dependent protein binding / peptidase activity / serine-type endopeptidase activity / calcium ion binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein homodimerization activity / extracellular space / extracellular region / nucleoplasm / identical protein binding / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Durvanger, Z. / Harmat, V. / Dobo, J. / Megyeri, M. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides. Authors: Durvanger, Z. / Boros, E. / Nagy, Z.A. / Hegedus, R. / Megyeri, M. / Dobo, J. / Gal, P. / Schlosser, G. / Angyan, A.F. / Gaspari, Z. / Perczel, A. / Harmat, V. / Mezo, G. / Menyhard, D.K. / Pal, G. #1: Journal: J Immunol. / Year: 2010 Title: Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant ...Title: Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation. Authors: Kocsis, A. / Kekesi, K.A. / Szasz, R. / Vegh, B.M. / Balczer, J. / Dobo, J. / Zavodszky, P. / Gal, P. / Pal, G. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 200.6 KB | Display | ![]() |
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PDB format | ![]() | 131 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3govS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 17508.240 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P48740, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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#2: Protein | Mass: 28028.834 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P48740, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
#3: Protein/peptide | Mass: 1471.765 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Peptide was developed by phage display technique based on the SFTI inhibitor (UniProt ID Q4GWU5) to selectively inhibit MASP-1 Source: (synth.) ![]() ![]() |
#4: Chemical | ChemComp-PEG / |
#5: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.45 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 0.1M Hepes, 42 w/v% PEG200, pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Dec 11, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9769 Å / Relative weight: 1 |
Reflection | Resolution: 2.42→29.52 Å / Num. obs: 17832 / % possible obs: 97.1 % / Redundancy: 7.83 % / Biso Wilson estimate: 64.31 Å2 / CC1/2: 0.999 / Rrim(I) all: 0.106 / Net I/σ(I): 14.74 |
Reflection shell | Resolution: 2.42→2.5 Å / Redundancy: 7.05 % / Num. unique obs: 1564 / CC1/2: 0.314 / Rrim(I) all: 2.08 / % possible all: 76.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3GOV Resolution: 2.42→19.85 Å / SU ML: 0.4648 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 34.8287 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 76.57 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.42→19.85 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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