PDBe 1ef0

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural insights into the protein splicing mechanism of PI-SceI.
J. Biol. Chem. 275 16408-13 (2000)
PMID: 10828056

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease PI-SceI Chains: A, B
Molecule details ›
Chains: A, B
Length: 462 amino acids
Theoretical weight: 51.8 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P17255 (Residues: 283-741; Coverage: 43%)
Gene names: CLS8, D1286, TFP1, VMA1, YDL185W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 59.003Å b: 101.683Å c: 86.765Å
α: 90° β: 93.51° γ: 90°
R-values:
R R work R free
0.231 0.231 0.281
Expression system: Escherichia coli