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Open data
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Basic information
Entry | Database: PDB / ID: 8gt7 | ||||||
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Title | Structure of falcipain and human Stefin A mutant complex | ||||||
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![]() | HYDROLASE / falcipain / stefin / complex | ||||||
Function / homology | ![]() MHC class II antigen presentation / negative regulation of peptidase activity / peptidase inhibitor complex / Neutrophil degranulation / food vacuole / Formation of the cornified envelope / peptide cross-linking / cornified envelope / cysteine-type endopeptidase inhibitor activity / keratinocyte differentiation ...MHC class II antigen presentation / negative regulation of peptidase activity / peptidase inhibitor complex / Neutrophil degranulation / food vacuole / Formation of the cornified envelope / peptide cross-linking / cornified envelope / cysteine-type endopeptidase inhibitor activity / keratinocyte differentiation / proteolysis involved in protein catabolic process / negative regulation of proteolysis / cell-cell adhesion / protease binding / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / cysteine-type endopeptidase activity / proteolysis / extracellular space / nucleoplasm / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chakraborty, S. / Biswas, S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of falcipain and human Stefin A complex Authors: Chakraborty, S. / Biswas, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 240.9 KB | Display | ![]() |
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PDB format | ![]() | 166.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 33.3 MB | Display | ![]() |
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Full document | ![]() | 33.7 MB | Display | |
Data in XML | ![]() | 54.5 KB | Display | |
Data in CIF | ![]() | 68.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8gt0C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Protein , 2 types, 4 molecules ACBD
#1: Protein | Mass: 27205.672 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q8I6U4, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases #2: Protein | Mass: 11048.478 Da / Num. of mol.: 2 / Mutation: K68R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Protein/peptide , 2 types, 2 molecules EF
#3: Protein/peptide | Mass: 1043.256 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#4: Protein/peptide | Mass: 987.151 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 8 types, 431 molecules ![](data/chem/img/GOL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/PG4.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/PE8.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/PG4.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/PE8.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-GOL / #6: Chemical | ChemComp-NA / #7: Chemical | ChemComp-PG4 / #8: Chemical | ChemComp-SO4 / #9: Chemical | ChemComp-PEG / #10: Chemical | ChemComp-PE8 / #11: Chemical | ChemComp-EDO / #12: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58.06 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop Details: 0.05 M cadmium chloride, 0.1 M Na HEPES pH 7.5 and 1.5 M sodium acetate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Dec 10, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9677 Å / Relative weight: 1 |
Reflection | Resolution: 3.28→44.02 Å / Num. obs: 14680 / % possible obs: 99.74 % / Redundancy: 6.2 % / Biso Wilson estimate: 88.6 Å2 / Rmerge(I) obs: 0.311 / Net I/σ(I): 4.7 |
Reflection shell | Resolution: 3.28→3.4 Å / Num. unique obs: 1447 / CC1/2: 0.368 |
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Processing
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Refinement | Method to determine structure: ![]() 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: 71.23 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.28→42.09 Å
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Refine LS restraints |
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LS refinement shell |
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