5sup

X-ray diffraction
2.6Å resolution

Crystal structure of the Sub2-Yra1 complex in association with RNA

Released:

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 trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct RNA molecule
Macromolecules (3 distinct):
ATP-dependent RNA helicase SUB2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 390 amino acids
Theoretical weight: 44.46 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07478 (Residues: 61-446; Coverage: 87%)
Gene names: SUB2, YDL084W
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases
RNA annealing protein YRA1 Chains: G, H, I
Molecule details ›
Chains: G, H, I
Length: 32 amino acids
Theoretical weight: 3.68 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12159 (Residues: 200-226; Coverage: 12%)
Gene names: D9481.2, D9509.1, YDR381W, YRA1
RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 15 nucleotides
Theoretical weight: 4.55 KDa

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3121
Unit cell:
a: 99.346Å b: 99.346Å c: 247.469Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.219 0.268
Expression system: Escherichia coli