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Open data
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Basic information
Entry | Database: PDB / ID: 5txc | ||||||
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Title | AtxE2 Isopeptidase - APO | ||||||
![]() | AtxE2 | ||||||
![]() | HYDROLASE / Lasso Peptide / Isopeptidase | ||||||
Function / homology | Hydrolases; Acting on peptide bonds (peptidases) / Peptidase S9, prolyl oligopeptidase, catalytic domain / Prolyl oligopeptidase family / Six-bladed beta-propeller, TolB-like / serine-type peptidase activity / Alpha/Beta hydrolase fold / proteolysis / cytoplasm / Lasso peptide isopeptidase AtxE2![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chekan, J.R. / Nair, S.K. | ||||||
![]() | ![]() Title: Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates. Authors: Chekan, J.R. / Koos, J.D. / Zong, C. / Maksimov, M.O. / Link, A.J. / Nair, S.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 273.5 KB | Display | ![]() |
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PDB format | ![]() | 227.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.5 KB | Display | ![]() |
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Full document | ![]() | 456.2 KB | Display | |
Data in XML | ![]() | 51.4 KB | Display | |
Data in CIF | ![]() | 74.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 78699.836 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48 / Gene: Astex_2444 / Production host: ![]() ![]() References: UniProt: E8RUP5, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.25 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 21% PEG3350, 0.4 M sodium chloride, 0.1 M Bis-Tris, pH 5.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 23, 2014 |
Radiation | Monochromator: diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 64978 / % possible obs: 98.6 % / Redundancy: 4.6 % / Rsym value: 0.138 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2.4→2.44 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.749 / Mean I/σ(I) obs: 4.3 / % possible all: 83.8 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.401→49.716 Å
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Refine LS restraints |
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LS refinement shell |
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