2jwn

Solution NMR

Solution NMR structure of the protease-resistent domain of Xenopus laevis ePABP2

Released:
Source organism: Xenopus laevis
Primary publication:
Structural basis for RNA recognition by a type II poly(A)-binding protein.
Proc Natl Acad Sci U S A 105 15317-22 (2008)
PMID: 18824697

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-180398 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Embryonic polyadenylate-binding protein 2-B Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 13.55 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6TY21 (Residues: 60-180; Coverage: 56%)
Gene names: Pabpn1l-b, epabp2-b, pabpnl1-b
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Torsion Angle Dynamics, Simulated Annealing
Expression system: Escherichia coli