4nql

X-ray diffraction
2.3Å resolution

The crystal structure of the DUB domain of AMSH orthologue, Sst2 from S. pombe, in complex with lysine 63-linked diubiquitin

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
AMSH-like protease sst2 Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 24.66 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9P371 (Residues: 221-435; Coverage: 49%)
Gene names: SPAC19B12.10, sst2
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Structure domains: Cytidine Deaminase, domain 2
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.6 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0CG50 (Residues: 609-684; Coverage: 10%)
Gene name: Ubc
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ubiquitin Chain: C
Molecule details ›
Chain: C
Length: 77 amino acids
Theoretical weight: 8.69 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0CG50 (Residues: 609-684; Coverage: 10%)
Gene name: Ubc
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 49.489Å b: 56.74Å c: 135.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.263
Expression system: Escherichia coli BL21