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Open data
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Basic information
Entry | Database: PDB / ID: 7ahp | ||||||
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Title | Crystal structure of Ixodes ricinus serpin - Iripin-3 | ||||||
![]() | (Putative salivary serpin) x 2 | ||||||
![]() | HYDROLASE INHIBITOR / Serpin / Inhibitor / Ixodes ricinus / HYDROLASE | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kascakova, B. / Kuta Smatanova, I. / Prudnikova, T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Iripin-3, a New Salivary Protein Isolated From Ixodes ricinus Ticks, Displays Immunomodulatory and Anti-Hemostatic Properties In Vitro Authors: Chlastakova, A. / Kotal, J. / Berankova, Z. / Kascakova, B. / Martins, L.A. / Langhansova, H. / Prudnikova, T. / Ederova, M. / Kotsyfakis, M. / Chmelar, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.9 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.6 KB | Display | ![]() |
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Full document | ![]() | 437.2 KB | Display | |
Data in XML | ![]() | 17.2 KB | Display | |
Data in CIF | ![]() | 24.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3ndaS 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 on special symmetry positions |
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Components
#1: Protein | Mass: 39157.332 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
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#2: Protein/peptide | Mass: 3712.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
#3: Chemical | #4: Water | ChemComp-HOH / | Compound details | Two protein chains result from protease cleavage (between residues 355 and 363) that is common for ...Two protein chains result from protease cleavage (between residues 355 and 363) that is common for serpins. After binding of the serpin reactive center loop (RCL) to protease and subsequent cleavage and insertion of RCL into beta-sheet A. Chain A corresponds to the N-terminal region generated by the proteolytic event and chain lowercase aa corresponds to the C-terminal region. | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.68 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 6.5 / Details: potassium thiocyanate, sodium cacodylate, PGA |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 17, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→48.32 Å / Num. obs: 34278 / % possible obs: 99.9 % / Redundancy: 1.573 % / CC1/2: 0.998 / Net I/σ(I): 0.1345 |
Reflection shell | Resolution: 1.95→2.07 Å / Num. unique obs: 889221 / CC1/2: 0.826 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3nda Resolution: 1.95→48.32 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.919 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.151 / ESU R Free: 0.138 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 89.72 Å2 / Biso mean: 24.264 Å2 / Biso min: 8.99 Å2
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Refinement step | Cycle: final / Resolution: 1.95→48.32 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→1.999 Å / Rfactor Rfree error: 0
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