PDBe 4trq

X-ray diffraction
3.1Å resolution

Crystal structure of Sac3/Thp1/Sem1

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Nuclear mRNA export protein SAC3 Chains: A, D
Molecule details ›
Chains: A, D
Length: 299 amino acids
Theoretical weight: 35.17 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46674 (Residues: 253-551; Coverage: 23%)
Gene names: LEP1, SAC3, YD8358.13, YDR159W
Nuclear mRNA export protein THP1 Chains: B, E
Molecule details ›
Chains: B, E
Length: 286 amino acids
Theoretical weight: 33.45 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q08231 (Residues: 170-455; Coverage: 63%)
Gene names: BUD29, O1140, THP1, YOL072W
Sequence domains: PCI domain
26S proteasome complex subunit SEM1 Chains: C, F
Molecule details ›
Chains: C, F
Length: 60 amino acids
Theoretical weight: 7.22 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O94742 (Residues: 30-89; Coverage: 67%)
Gene names: DSH1, SEM1, YDR363W-A

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41212
Unit cell:
a: 125.741Å b: 125.741Å c: 268.367Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.238
Expression system: Escherichia coli BL21(DE3)