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- PDB-7oxy: Crystal structure of depupylase Dop in complex with Pup and AMP-PCP -
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Open data
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Basic information
Entry | Database: PDB / ID: 7oxy | ||||||
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Title | Crystal structure of depupylase Dop in complex with Pup and AMP-PCP | ||||||
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![]() | HYDROLASE / depupylase / ATP hydrolysis / deamidase / Pup binding | ||||||
Function / homology | ![]() protein pupylation / hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides / Hydrolases; Acting on peptide bonds (peptidases) / proteasome binding / proteasomal protein catabolic process / modification-dependent protein catabolic process / protein tag activity / peptidase activity / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Cui, H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation. Authors: Cui, H. / Muller, A.U. / Leibundgut, M. / Tian, J. / Ban, N. / Weber-Ban, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 130.5 KB | Display | ![]() |
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PDB format | ![]() | 97.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 23 KB | Display | |
Data in CIF | ![]() | 34.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7oxvC ![]() 7oy3C ![]() 7oyfC ![]() 7oyhC ![]() 5lrtS S: Starting model for refinement C: citing same article ( |
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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
-Protein / Protein/peptide , 2 types, 2 molecules AB
#1: Protein | Mass: 57288.332 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The C-terminal ENLYFQ fragment is a leftover from TEV clevage site. Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: A0LU48, Hydrolases; Acting on peptide bonds (peptidases) |
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#2: Protein/peptide | Mass: 3198.405 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This is only the C-terminal half of the Pup protein. Source: (synth.) ![]() References: UniProt: A0LU49 |
-Non-polymers , 7 types, 345 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/ACP.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/ACP.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-EDO / #5: Chemical | ChemComp-ACP / | #6: Chemical | ChemComp-ACT / #7: Chemical | #8: Chemical | #9: 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: 2.95 Å3/Da / Density % sol: 58.36 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 100 mM Tris-acetate pH 7.0-8.5, 10 mM AMP-PCP, 40 mM MgCl2 and 0.75-1.0 M KH2PO4 PH range: 7.0-8.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 29, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→46.19 Å / Num. obs: 86165 / % possible obs: 99.98 % / Redundancy: 20.2 % / CC1/2: 1 / Net I/σ(I): 21.3 |
Reflection shell | Resolution: 1.65→1.709 Å / Num. unique obs: 8506 / CC1/2: 0.746 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5LRT Resolution: 1.65→46.189 Å / SU ML: 0.19 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 19.62 / Stereochemistry target values: ML
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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 max: 100.13 Å2 / Biso mean: 33.4008 Å2 / Biso min: 18.01 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.65→46.189 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %
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