6sh7

X-ray diffraction
2.21Å resolution

Crystal structure of the human DEAH-helicase DHX15 in complex with the NKRF G-patch

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for DEAH-helicase activation by G-patch proteins.
Proc. Natl. Acad. Sci. U.S.A. 117 7159-7170 (2020)
PMID: 32179686

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 Chain: A
Molecule details ›
Chain: A
Length: 689 amino acids
Theoretical weight: 79.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O43143 (Residues: 113-795; Coverage: 86%)
Gene names: DBP1, DDX15, DHX15
Sequence domains:
NF-kappa-B-repressing factor Chain: B
Molecule details ›
Chain: B
Length: 67 amino acids
Theoretical weight: 7.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15226 (Residues: 541-603; Coverage: 9%)
Gene names: ITBA4, NKRF, NRF
Sequence domains: G-patch domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 82.243Å b: 90.024Å c: 213.885Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.251
Expression system: Escherichia coli BL21(DE3)