5b16

X-ray diffraction
3.2Å resolution

X-ray structure of DROSHA in complex with the C-terminal tail of DGCR8.

Released:
Source organism: Homo sapiens
Primary publication:
Structure of Human DROSHA.
Cell 164 81-90 (2016)
PMID: 26748718

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonuclease 3 Chain: A
Molecule details ›
Chain: A
Length: 986 amino acids
Theoretical weight: 108.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9NRR4 (Residues: 411-1365; Coverage: 70%)
Gene names: DROSHA, RN3, RNASE3L, RNASEN
Sequence domains:
Microprocessor complex subunit DGCR8 Chains: B, C
Molecule details ›
Chains: B, C
Length: 39 amino acids
Theoretical weight: 4.59 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q8WYQ5 (Residues: 728-750; Coverage: 3%)
Gene names: C22orf12, DGCR8, DGCRK6, LP4941

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2
Unit cell:
a: 117.254Å b: 118.136Å c: 122.296Å
α: 90° β: 102.07° γ: 90°
R-values:
R R work R free
0.267 0.267 0.3
Expression system: Homo sapiens