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- PDB-6hh5: ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in comple... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6hh5 | ||||||
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Title | ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-HPM | ||||||
![]() | ADP-ribosylhydrolase like 2 | ||||||
![]() | HYDROLASE / ADP-ribosylation / ADP-ribose / ADPRHL2 / ADP-ribosylhydrolase like 2 / ADP-HPM | ||||||
Function / homology | ![]() peptidyl-serine ADP-deribosylation / poly(ADP-ribose) glycohydrolase / poly(ADP-ribose) glycohydrolase activity / negative regulation of necroptotic process / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / chromosome / mitochondrial matrix / DNA repair / magnesium ion binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ariza, A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition. Authors: Rack, J.G.M. / Ariza, A. / Drown, B.S. / Henfrey, C. / Bartlett, E. / Shirai, T. / Hergenrother, P.J. / Ahel, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 281.8 KB | Display | ![]() |
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PDB format | ![]() | 224.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 28.5 KB | Display | |
Data in CIF | ![]() | 40.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6g1pC ![]() 6g1qC ![]() 6g28C ![]() 6g2aC ![]() 6hgzC ![]() 6hh3C ![]() 6hh4C ![]() 6hh6C ![]() 6hozC ![]() 2fozS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: _ / Auth seq-ID: 9 - 353 / Label seq-ID: 3 - 347
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Components
#1: Protein | Mass: 38289.520 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.94 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 200 MM AMMONIUM ACETATE, 25 % (W/V), PEG4000, 100 MM CITRATE PH 5.6 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Aug 8, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→44.5 Å / Num. obs: 51249 / % possible obs: 99.8 % / Redundancy: 8.5 % / CC1/2: 0.995 / Rmerge(I) obs: 0.105 / Rpim(I) all: 0.057 / Rrim(I) all: 0.119 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 1.95→2 Å / Redundancy: 8.6 % / Rmerge(I) obs: 1.837 / Mean I/σ(I) obs: 0.9 / Num. unique obs: 3716 / CC1/2: 0.814 / Rpim(I) all: 0.977 / Rrim(I) all: 2.087 / % possible all: 99.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2FOZ Resolution: 1.95→41.46 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.966 / SU B: 11.706 / SU ML: 0.151 / Cross valid method: THROUGHOUT / ESU R: 0.166 / ESU R Free: 0.142 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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 mean: 59.438 Å2
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Refinement step | Cycle: 1 / Resolution: 1.95→41.46 Å
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Refine LS restraints |
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