› 5bxo

X-ray diffraction
1.33Å resolution

Human Tankyrase-2 in Complex with Macrocyclised Extended Peptide cp4n2m3

Released:
DOI: 10.2210/pdb5bxo/pdb
PDB entry 5bxo coloured by chain, front view.
PDB entry 5bxo coloured by chain, side view.
PDB entry 5bxo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Macrocyclized Extended Peptides: Inhibiting the Substrate-Recognition Domain of Tankyrase.
Xu W, Lau YH, Fischer G, Tan YS, Chattopadhyay A, de la Roche M, Hyvönen M, Verma C, Spring DR, Itzhaki LS
J Am Chem Soc 139 2245-2256 (2017)
PMID: 28084734

Function and Biology Details

Reaction catalysed: 
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190550 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Poly [ADP-ribose] polymerase tankyrase-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 17.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H2K2 (Residues: 488-649; Coverage: 14%)
Gene names: PARP5B, TANK2, TNKL, TNKS2
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Ankyrin repeat-containing domain
Poly [ADP-ribose] polymerase tankyrase-2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 10 amino acids
Theoretical weight: 829 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9H2K2 (Residues: 5-12; Coverage: 1%)
Gene names: PARP5B, TANK2, TNKL, TNKS2

Ligands and Environments

3 bound ligands:
Ligand SO4 6 x SO4
Ligand DMS 3 x DMS
Ligand 4XP 2 x 4XP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P1
Unit cell:
a: 29.823Å b: 46.014Å c: 54.472Å
α: 78.45° β: 88.99° γ: 72.35°
R-values:
R R work R free
0.176 0.175 0.203
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

4 review citations

Using Peptidomimetics and Constrained Peptides as Valuable Tools for Inhibiting Protein⁻Protein Interactions.
Robertson et al. (2018)
3 more

4 mentions without citation

Regulation of Wnt/β-catenin signalling by tankyrase-dependent poly(ADP-ribosyl)ation and scaffolding.
Mariotti et al. (2017)
3 more