1zhi

X-ray diffraction
2.7Å resolution

Complex of the S. cerevisiae Orc1 and Sir1 interacting domains

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing.
Proc Natl Acad Sci U S A 102 8489-94 (2005)
PMID: 15932939

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-149361 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Origin recognition complex subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 26.1 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P54784 (Residues: 1-219; Coverage: 24%)
Gene names: ORC1, YML065W
Sequence domains: BAH domain
Structure domains: SH3 type barrels.
Regulatory protein SIR1 Chain: B
Molecule details ›
Chain: B
Length: 138 amino acids
Theoretical weight: 16.16 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P21691 (Residues: 456-587; Coverage: 20%)
Gene names: SIR1, YKR101W
Sequence domains: Sir1, ORC-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P6122
Unit cell:
a: 72.151Å b: 72.151Å c: 310.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.231 0.293
Expression system: Escherichia coli BL21