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- PDB-4pnm: Crystal Structure of human Tankyrase 2 in complex with Nu1025. -

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Basic information

Entry
Database: PDB / ID: 4pnm
TitleCrystal Structure of human Tankyrase 2 in complex with Nu1025.
ComponentsTankyrase-2
KeywordsTRANSFERASE / poly(ADP-ribosylation) polymerase (PARP)
Function / homology
Function and homology information


XAV939 stabilizes AXIN / protein localization to chromosome, telomeric region / NAD+ ADP-ribosyltransferase / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / pericentriolar material / protein poly-ADP-ribosylation / NAD+-protein ADP-ribosyltransferase activity / positive regulation of telomere capping / protein ADP-ribosylation ...XAV939 stabilizes AXIN / protein localization to chromosome, telomeric region / NAD+ ADP-ribosyltransferase / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / pericentriolar material / protein poly-ADP-ribosylation / NAD+-protein ADP-ribosyltransferase activity / positive regulation of telomere capping / protein ADP-ribosylation / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ ADP-ribosyltransferase activity / regulation of multicellular organism growth / positive regulation of telomere maintenance via telomerase / TCF dependent signaling in response to WNT / Degradation of AXIN / multicellular organism growth / Wnt signaling pathway / protein polyubiquitination / Regulation of PTEN stability and activity / nuclear envelope / positive regulation of canonical Wnt signaling pathway / protein N-terminus binding / chromosome, telomeric region / Ub-specific processing proteases / Golgi membrane / perinuclear region of cytoplasm / enzyme binding / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Phosphoenolpyruvate Carboxykinase; domain 3 - #10 / Ankyrin repeats (many copies) / Phosphoenolpyruvate Carboxykinase; domain 3 / Ankyrin repeats (many copies) / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / SAM domain (Sterile alpha motif) / Ankyrin repeat / SAM domain profile. ...Phosphoenolpyruvate Carboxykinase; domain 3 - #10 / Ankyrin repeats (many copies) / Phosphoenolpyruvate Carboxykinase; domain 3 / Ankyrin repeats (many copies) / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / SAM domain (Sterile alpha motif) / Ankyrin repeat / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Ankyrin repeats (3 copies) / Ankyrin repeat region circular profile. / Ankyrin repeat profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
8-HYDROXY-2-METHYL-3-HYDRO-QUINAZOLIN-4-ONE / Poly [ADP-ribose] polymerase tankyrase-2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.19 Å
AuthorsQiu, W. / Lam, R. / Romanov, V. / Gordon, R. / Gebremeskel, S. / Vodsedalek, J. / Thompson, C. / Beletskaya, I. / Battaile, K.P. / Pai, E.F. / Chirgadze, N.Y.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2014
Title: Insights into the binding of PARP inhibitors to the catalytic domain of human tankyrase-2.
Authors: Qiu, W. / Lam, R. / Voytyuk, O. / Romanov, V. / Gordon, R. / Gebremeskel, S. / Vodsedalek, J. / Thompson, C. / Beletskaya, I. / Battaile, K.P. / Pai, E.F. / Rottapel, R. / Chirgadze, N.Y.
History
DepositionMay 23, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 15, 2014Provider: repository / Type: Initial release
Revision 1.1Jan 7, 2015Group: Database references
Revision 1.2Feb 4, 2015Group: Derived calculations

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tankyrase-2
B: Tankyrase-2
C: Tankyrase-2
D: Tankyrase-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)105,03614
Polymers103,9454
Non-polymers1,09010
Water6,197344
1
A: Tankyrase-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,2283
Polymers25,9861
Non-polymers2422
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Tankyrase-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,2283
Polymers25,9861
Non-polymers2422
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Tankyrase-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,2904
Polymers25,9861
Non-polymers3043
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Tankyrase-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,2904
Polymers25,9861
Non-polymers3043
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)72.960, 79.250, 153.830
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Detailsmonomer

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Components

#1: Protein
Tankyrase-2 / / TANK2 / ADP-ribosyltransferase diphtheria toxin-like 6 / ARTD6 / Poly [ADP-ribose] polymerase 5B / ...TANK2 / ADP-ribosyltransferase diphtheria toxin-like 6 / ARTD6 / Poly [ADP-ribose] polymerase 5B / TNKS-2 / TRF1-interacting ankyrin-related ADP-ribose polymerase 2 / Tankyrase II / Tankyrase-like protein / Tankyrase-related protein


Mass: 25986.291 Da / Num. of mol.: 4 / Fragment: PARP, catalytic domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNKS2, PARP5B, TANK2, TNKL / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H2K2, NAD+ ADP-ribosyltransferase
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-NU1 / 8-HYDROXY-2-METHYL-3-HYDRO-QUINAZOLIN-4-ONE / NU1025


Mass: 176.172 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C9H8N2O2
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 344 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.14 Å3/Da / Density % sol: 42.5 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.2M NaCl, 0.1M Sodium, Hepes buffer at pH7.5, 12-15% iso-propanol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 19, 2010 / Details: mirrors
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.19→79.25 Å / Num. obs: 46699 / % possible obs: 99.9 % / Redundancy: 7.05 % / Biso Wilson estimate: 36.76 Å2 / Rmerge(I) obs: 0.099 / Net I/σ(I): 13.44 / Num. measured all: 329620
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. possibleNum. unique obsNet I/σ(I) obs% possible all
2.19-2.246.750.56242023832.8298.5
2.24-2.297.370.519281928183.45100
2.29-2.347.370.488257825763.5899.9
2.34-2.397.380.461234423433.93100
2.39-2.457.30.418260926094.36100
2.45-2.527.230.389270127014.71100
2.52-2.597.130.335240924095.28100
2.59-2.676.890.309248424835.81100
2.67-2.766.460.262246124576.599.8
2.76-2.877.090.224259825988.1100
2.87-2.996.990.182242624259.7100
2.99-3.136.690.1372364236412100
3.13-3.37.470.1172394239315.65100
3.3-3.517.380.0872340233919.92100
3.51-3.797.270.072378237824.59100
3.79-4.197.010.0562396239429.1599.9
4.19-4.826.660.0462351234633.6199.8
4.82-6.126.490.0472340233731.6499.9
6.12-79.256.810.0392354234637.2699.7

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Processing

Software
NameVersionClassification
XDS2005/3data reduction
BUSTER-TNTBUSTER 2.10.0refinement
PDB_EXTRACT3.14data extraction
BUSTER2.10.0refinement
XPREPdata scaling
RefinementResolution: 2.19→76.92 Å / Cor.coef. Fo:Fc: 0.8968 / Cor.coef. Fo:Fc free: 0.8814 / SU R Cruickshank DPI: 0.272 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.282 / SU Rfree Blow DPI: 0.207 / SU Rfree Cruickshank DPI: 0.206
RfactorNum. reflection% reflectionSelection details
Rfree0.2437 1070 2.3 %RANDOM
Rwork0.2035 ---
obs0.2044 46616 99.82 %-
Displacement parametersBiso max: 123.09 Å2 / Biso mean: 43.63 Å2 / Biso min: 20.47 Å2
Baniso -1Baniso -2Baniso -3
1--19.2034 Å20 Å20 Å2
2--0.3555 Å20 Å2
3---18.8479 Å2
Refine analyzeLuzzati coordinate error obs: 0.291 Å
Refinement stepCycle: final / Resolution: 2.19→76.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6554 0 64 344 6962
Biso mean--36.95 48.73 -
Num. residues----815
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d3094SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes152HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1029HARMONIC5
X-RAY DIFFRACTIONt_it6831HARMONIC20
X-RAY DIFFRACTIONt_nbd4SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion808SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact7606SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d6831HARMONIC20.007
X-RAY DIFFRACTIONt_angle_deg9196HARMONIC20.92
X-RAY DIFFRACTIONt_omega_torsion3.09
X-RAY DIFFRACTIONt_other_torsion3.14
LS refinement shellResolution: 2.19→2.25 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2761 82 2.45 %
Rwork0.2419 3271 -
all0.2427 3353 -
obs--99.82 %

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