- PDB-5v7w: Crystal structure of human PARP14 bound to 2-{[(1-methylpiperidin... -
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Basic information
Entry
Database: PDB / ID: 5v7w
Title
Crystal structure of human PARP14 bound to 2-{[(1-methylpiperidin-4-yl)methyl]amino}-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one inhibitor
Components
Poly [ADP-ribose] polymerase 14
Keywords
TRANSFERASE/TRANSFERASE INHIBITOR / HUMAN PARP14 / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information
positive regulation of interleukin-4-mediated signaling pathway / negative regulation of tyrosine phosphorylation of STAT protein / Nicotinamide salvaging / Maturation of nucleoprotein / Maturation of nucleoprotein / protein poly-ADP-ribosylation / negative regulation of type II interferon-mediated signaling pathway / NAD+-protein ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ ADP-ribosyltransferase activity ...positive regulation of interleukin-4-mediated signaling pathway / negative regulation of tyrosine phosphorylation of STAT protein / Nicotinamide salvaging / Maturation of nucleoprotein / Maturation of nucleoprotein / protein poly-ADP-ribosylation / negative regulation of type II interferon-mediated signaling pathway / NAD+-protein ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ ADP-ribosyltransferase activity / NAD+ binding / positive regulation of tyrosine phosphorylation of STAT protein / nucleotidyltransferase activity / transcription corepressor activity / negative regulation of gene expression / innate immune response / enzyme binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.2398 Å / Relative weight: 1
Reflection
Resolution: 2.6→72.45 Å / Num. obs: 14247 / % possible obs: 99.88 % / Redundancy: 3.7 % / Net I/σ(I): 9.8
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0049
refinement
HKL-2000
datareduction
HKL-2000
datascaling
MOLREP
phasing
Refinement
Resolution: 2.65→72.45 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.92 / SU B: 35.708 / SU ML: 0.311 / Cross valid method: THROUGHOUT / ESU R Free: 0.329 / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.26595
758
5.1 %
RANDOM
Rwork
0.20351
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obs
0.20678
14247
99.88 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å