4ilg

X-ray diffraction
2.1Å resolution

Crystal structure of Aar2p in complex with the Prp8p RNaseH and Jab1/MPN domains

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-152276 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
A1 cistron-splicing factor AAR2 Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 40.22 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P32357 (Residues: 1-355; Coverage: 96%)
Gene names: AAR2, YBL06.06, YBL0611, YBL074C
Sequence domains:
Structure domains:
Pre-mRNA-splicing factor 8 Chain: B
Molecule details ›
Chain: B
Length: 258 amino acids
Theoretical weight: 29.5 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P33334 (Residues: 1836-2090; Coverage: 11%)
Gene names: DBF3, DNA39, PRP8, RNA8, SLT21, USA2, YHR165C
Sequence domains: PRP8 domain IV core
Structure domains:
Pre-mRNA-splicing factor 8 Chain: C
Molecule details ›
Chain: C
Length: 270 amino acids
Theoretical weight: 30.49 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P33334 (Residues: 2147-2413; Coverage: 11%)
Gene names: DBF3, DNA39, PRP8, RNA8, SLT21, USA2, YHR165C
Sequence domains: PROCT (NUC072) domain
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 84.768Å b: 63.739Å c: 110.518Å
α: 90° β: 95.39° γ: 90°
R-values:
R R work R free
0.182 0.18 0.228
Expression system: Escherichia coli