› 4dk6

X-ray diffraction
2.65Å resolution

Function and Biology Details

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-212675 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
single domain antibody VHH Chains: A, B
Molecule details ›
Chains: A, B
Length: 133 amino acids
Theoretical weight: 14.77 KDa
Source organism: Lama glama
Expression system: Escherichia coli BL21(DE3)
Structure domains: Immunoglobulins
C2H2-type domain-containing protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 105 amino acids
Theoretical weight: 11.44 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q95W15 (Residues: 624-657, 696-762; Coverage: 13%)
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: C2
Unit cell:
a: 173.026Å b: 40.882Å c: 61.281Å
α: 90° β: 92.55° γ: 90°
R-values:
R R work R free
0.226 0.224 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Trypanosome RNA editing: the complexity of getting U in and taking U out.
Read et al. (2016)
1 more

1 mention without citation

The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA-editing ligase L2.
Park et al. (2012)