› 5o3j

X-ray diffraction
2.97Å resolution

Crystal structure of TIA-1 RRM2 in complex with RNA

Released:
DOI: 10.2210/pdb5o3j/pdb
PDB entry 5o3j coloured by chain, front view.
PDB entry 5o3j coloured by chain, side view.
PDB entry 5o3j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
Angew Chem Int Ed Engl 56 9322-9325 (2017)
PMID: 28636238

Function and Biology Details

Biochemical function:
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-152018 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Cytotoxic granule associated RNA binding protein TIA1 Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 8.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31483 (Residues: 104-181; Coverage: 20%)
Gene name: TIA1
Sequence domains: RNA recognition motif
RNA (5'-R(P*UP*UP*C)-3') Chain: B
Molecule details ›
Chain: B
Length: 3 nucleotides
Theoretical weight: 873 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P65
Unit cell:
a: 44.31Å b: 44.31Å c: 85.72Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.254 0.251 0.312
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Hybrid methods for combined experimental and computational determination of protein structure.
Seffernick et al. (2020)
3 more

4 mentions without citation

Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.
Vogl et al. (2021)
3 more