6rr0

X-ray diffraction
2.18Å resolution

Crystal structure of the Sir4 H-BRCT domain in complex with Ubp10 pT123 peptide

Released:

Function and Biology Details

Reaction catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-146018 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Regulatory protein SIR4 Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 127 amino acids
Theoretical weight: 14.87 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11978 (Residues: 961-1085; Coverage: 9%)
Gene names: ASD1, SIR4, STE9, UTH2, YD9934.12, YDR227W
Ubiquitin carboxyl-terminal hydrolase 10 Chains: H, I, J, K, L, M, N
Molecule details ›
Chains: H, I, J, K, L, M, N
Length: 12 amino acids
Theoretical weight: 1.33 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P53874 (Residues: 117-128; Coverage: 2%)
Gene names: DOT4, N1619, UBP10, YNL186W

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 70.04Å b: 75.28Å c: 95.91Å
α: 90° β: 97.24° γ: 90°
R-values:
R R work R free
0.198 0.196 0.218
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided