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- PDB-7pwq: PARP15 catalytic domain in complex with OUL240 -

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Basic information

Entry
Database: PDB / ID: 7pwq
TitlePARP15 catalytic domain in complex with OUL240
ComponentsProtein mono-ADP-ribosyltransferase PARP15
KeywordsTRANSFERASE / ADP-ribosyltransferase / Inhibitor / Complex
Function / homology
Function and homology information


NAD+-protein-aspartate ADP-ribosyltransferase activity / protein poly-ADP-ribosylation / NAD+-protein-glutamate ADP-ribosyltransferase activity / NAD+-protein mono-ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ poly-ADP-ribosyltransferase activity / NAD+ binding / nucleotidyltransferase activity / transcription corepressor activity / negative regulation of gene expression ...NAD+-protein-aspartate ADP-ribosyltransferase activity / protein poly-ADP-ribosylation / NAD+-protein-glutamate ADP-ribosyltransferase activity / NAD+-protein mono-ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ poly-ADP-ribosyltransferase activity / NAD+ binding / nucleotidyltransferase activity / transcription corepressor activity / negative regulation of gene expression / negative regulation of transcription by RNA polymerase II / nucleus / cytoplasm
Similarity search - Function
: / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / Appr-1"-p processing enzyme / Macro domain / Macro domain profile. / Macro domain / Macro domain-like
Similarity search - Domain/homology
6-(cyclohexylmethoxy)phthalazine-1,4-dione / Protein mono-ADP-ribosyltransferase PARP15
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsMaksimainen, M.M. / Lehtio, L.
Funding support Finland, 2items
OrganizationGrant numberCountry
Academy of Finland287063 and 294085 Finland
Jane and Aatos Erkko Foundation Finland
CitationJournal: Eur.J.Med.Chem. / Year: 2022
Title: Potent 2,3-dihydrophthalazine-1,4-dione derivatives as dual inhibitors for mono-ADP-ribosyltransferases PARP10 and PARP15.
Authors: Nizi, M.G. / Maksimainen, M.M. / Murthy, S. / Massari, S. / Alaviuhkola, J. / Lippok, B.E. / Sowa, S.T. / Galera-Prat, A. / Prunskaite-Hyyrylainen, R. / Luscher, B. / Korn, P. / Lehtio, L. / Tabarrini, O.
History
DepositionOct 7, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 11, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein mono-ADP-ribosyltransferase PARP15
B: Protein mono-ADP-ribosyltransferase PARP15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,2694
Polymers50,8792
Non-polymers3902
Water6,053336
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: light scattering, The dimer formation has been confirmed by Venkannagari et al. https://pubmed.ncbi.nlm.nih.gov/23485441/
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2450 Å2
ΔGint-22 kcal/mol
Surface area19270 Å2
MethodPISA
Unit cell
Length a, b, c (Å)45.720, 69.480, 161.650
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Protein mono-ADP-ribosyltransferase PARP15 / ADP-ribosyltransferase diphtheria toxin-like 7 / ARTD7 / B-aggressive lymphoma protein 3 / Poly ...ADP-ribosyltransferase diphtheria toxin-like 7 / ARTD7 / B-aggressive lymphoma protein 3 / Poly [ADP-ribose] polymerase 15 / PARP-15


Mass: 25439.459 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PARP15, BAL3 / Production host: Escherichia coli (E. coli)
References: UniProt: Q460N3, Transferases; Glycosyltransferases; Pentosyltransferases
#2: Chemical ChemComp-8A8 / 6-(cyclohexylmethoxy)phthalazine-1,4-dione


Mass: 272.299 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C15H16N2O3 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 336 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.52 Å3/Da / Density % sol: 51.25 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / Details: 0.2 M ammonium chloride pH 7.5, 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.96546 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Nov 9, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.96546 Å / Relative weight: 1
ReflectionResolution: 1.7→50 Å / Num. obs: 57216 / % possible obs: 99.3 % / Redundancy: 3.9 % / CC1/2: 0.962 / Net I/σ(I): 5.55
Reflection shellResolution: 1.7→1.74 Å / Num. unique obs: 4189 / CC1/2: 0.796

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
XSCALEdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7OTH

7oth


Resolution: 1.7→44.03 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.935 / SU B: 2.101 / SU ML: 0.069 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.097 / ESU R Free: 0.097 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2177 2861 5 %RANDOM
Rwork0.1852 ---
obs0.1869 54355 99.27 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 79.76 Å2 / Biso mean: 19.278 Å2 / Biso min: 9.05 Å2
Baniso -1Baniso -2Baniso -3
1--0.48 Å2-0 Å2-0 Å2
2--0.21 Å2-0 Å2
3---0.26 Å2
Refinement stepCycle: final / Resolution: 1.7→44.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3190 0 28 336 3554
Biso mean--19.6 29.04 -
Num. residues----393
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0133373
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173085
X-RAY DIFFRACTIONr_angle_refined_deg1.4971.6624585
X-RAY DIFFRACTIONr_angle_other_deg1.3451.5887112
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.7455408
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.7422.449196
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.93515559
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.8071521
X-RAY DIFFRACTIONr_chiral_restr0.0720.2428
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.023888
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02852
LS refinement shellResolution: 1.7→1.744 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.267 209 -
Rwork0.266 3974 -
all-4183 -
obs--99.76 %

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