3b6e

X-ray diffraction
1.6Å resolution

Crystal structure of human DECH-box RNA Helicase MDA5 (Melanoma differentiation-associated protein 5), DECH-domain

Released:
Source organism: Homo sapiens
Entry authors: Karlberg T, Welin M, Arrowsmith CH, Berglund H, Busam RD, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Johansson I, Kallas A, Kotenyova T, Lehtio L, Moche M, Nilsson ME, Nordlund P, Nyman T, Persson C, Sagemark J, Svensson L, Thorsell AG, Tresaugues L, Van Den Berg S, Weigelt J, Holmberg-Schiavone L, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interferon-induced helicase C domain-containing protein 1 Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 24.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BYX4 (Residues: 277-490; Coverage: 21%)
Gene names: IFIH1, MDA5, RH116
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6522
Unit cell:
a: 72.83Å b: 72.83Å c: 182.78Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.204
Expression system: Escherichia coli