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- PDB-4utn: Crystal structure of zebrafish Sirtuin 5 in complex with succinyl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4utn | ||||||
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Title | Crystal structure of zebrafish Sirtuin 5 in complex with succinylated CPS1-peptide | ||||||
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![]() | HYDROLASE / REGULATORY ENZYME / ROSSMANN-FOLD / ZINC-BINDING | ||||||
Function / homology | ![]() Transcriptional activation of mitochondrial biogenesis / regulation of ketone biosynthetic process / peptidyl-lysine demalonylation / protein desuccinylation / peptidyl-lysine desuccinylation / protein-glutaryllysine deglutarylase activity / protein-malonyllysine demalonylase activity / protein-succinyllysine desuccinylase activity / NAD-dependent histone deacetylase activity / heterocyclic compound binding ...Transcriptional activation of mitochondrial biogenesis / regulation of ketone biosynthetic process / peptidyl-lysine demalonylation / protein desuccinylation / peptidyl-lysine desuccinylation / protein-glutaryllysine deglutarylase activity / protein-malonyllysine demalonylase activity / protein-succinyllysine desuccinylase activity / NAD-dependent histone deacetylase activity / heterocyclic compound binding / NAD+ binding / acyl binding / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / transferase activity / mitochondrion / zinc ion binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pannek, M. / Gertz, M. / Steegborn, C. | ||||||
![]() | ![]() Title: Chemical Probing of the Human Sirtuin 5 Active Site Reveals its Substrate Acyl Specificity and Peptide-Based Inhibitors. Authors: Roessler, C. / Nowak, T. / Pannek, M. / Gertz, M. / Nguyen, G.T. / Scharfe, M. / Born, I. / Sippl, W. / Steegborn, C. / Schutkowski, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 222.7 KB | Display | ![]() |
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PDB format | ![]() | 180.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480.7 KB | Display | ![]() |
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Full document | ![]() | 485.2 KB | Display | |
Data in XML | ![]() | 21.1 KB | Display | |
Data in CIF | ![]() | 28.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4utrC ![]() 4utvC ![]() 4utxC ![]() 4utzC ![]() 4uu7C ![]() 4uu8C ![]() 4uuaC ![]() 4uubC ![]() 2nyrS C: citing same article ( 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.74826, -0.5507, -0.36991), Vector: |
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Components
-Protein / Protein/peptide , 2 types, 3 molecules ABD
#1: Protein | Mass: 30423.785 Da / Num. of mol.: 2 / Fragment: CATALYTIC CORE, RESIDUES 30-298 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q6DHI5, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides #2: Protein/peptide | | Mass: 1068.177 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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-Non-polymers , 5 types, 22 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/EPE.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EPE.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | ChemComp-EPE / | #5: Chemical | ChemComp-DMS / | #6: Chemical | ChemComp-EDO / | #7: Water | ChemComp-HOH / | |
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-Details
Sequence details | BENZOYLATE |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57 % / Description: NONE |
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Crystal grow | pH: 7.4 / Details: 20% PEG3350, 0.1 M HEPES PH 7.4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 14, 2012 / Details: MIRROR |
Radiation | Monochromator: SI111 CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 3→100 Å / Num. obs: 15155 / % possible obs: 99.9 % / Observed criterion σ(I): 1.7 / Redundancy: 8.1 % / Rmerge(I) obs: 0.18 / Net I/σ(I): 11.2 |
Reflection shell | Resolution: 3→3.1 Å / Redundancy: 8.5 % / Rmerge(I) obs: 1.34 / Mean I/σ(I) obs: 1.7 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2NYR Resolution: 3→75.73 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.902 / SU B: 43.64 / SU ML: 0.381 / Cross valid method: THROUGHOUT / ESU R Free: 0.44 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED. STRUCTURE REFINED USING PROSMART WITH PDB-ID 3RIY R.A. NICHOLLS, F. LONG AND G.N. MURSHUDOV (2012) LOW RESOLUTION ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED. STRUCTURE REFINED USING PROSMART WITH PDB-ID 3RIY R.A. NICHOLLS, F. LONG AND G.N. MURSHUDOV (2012) LOW RESOLUTION REFINEMENT TOOLS IN REFMAC5. ACTA CRYST. D.
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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: 70.934 Å2
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Refinement step | Cycle: LAST / Resolution: 3→75.73 Å
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Refine LS restraints |
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