› 4e5r

X-ray diffraction
1.9Å resolution

Crystal Structure of Frog DGCR8 Dimerization Domain

Released:
DOI: 10.2210/pdb4e5r/pdb
PDB entry 4e5r coloured by chain, front view.
PDB entry 4e5r coloured by chain, side view.
PDB entry 4e5r coloured by chain, top view.
Source organism: Xenopus laevis
Primary publication:
Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8.
Senturia R, Laganowsky A, Barr I, Scheidemantle BD, Guo F
PLoS One 7 e39688 (2012)
PMID: 22768307

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DGCR8 microprocessor complex subunit Chain: A
Molecule details ›
Chain: A
Length: 56 amino acids
Theoretical weight: 6.38 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6IRB5 (Residues: 300-355; Coverage: 7%)
Gene names: MGC78846, dgcr8, dgcr8.L
Structure domains: Ubiquitin Ligase Nedd4; Chain: W;

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 39.891Å b: 39.891Å c: 82.125Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.228
Expression system: Escherichia coli

Quick links

Citations

3 review citations

MicroRNA Machinery Genes as Novel Biomarkers for Cancer.
Huang et al. (2014)
2 more

1 mention without citation

Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8.
Senturia et al. (2012)