X-ray diffraction
1.15Å resolution

PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of human PARP14 Macrodomain 3 in complex with FMOPL000385a

Source organism: Homo sapiens
Entry authors: Schuller M, Talon R, Krojer T, Brandao-Neto J, Douangamath A, Zhang R, von Delft F, Schuler H, Kessler B, Knapp S, Bountra C, Arrowsmith CH, Edwards A, Elkins J

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Protein mono-ADP-ribosyltransferase PARP14 Chain: A
Molecule details ›
Chain: A
Length: 183 amino acids
Theoretical weight: 19.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q460N5 (Residues: 1208-1388; Coverage: 10%)
Gene names: BAL2, KIAA1268, PARP14
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 34.399Å b: 41.583Å c: 111.38Å
α: 90° β: 90° γ: 90°
R R work R free
0.141 0.14 0.174
Expression system: Escherichia coli