6hei

X-ray diffraction
1.64Å resolution

Structure of the catalytic domain of USP28 (insertion deleted) bound to Ubiquitin-PA

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).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 28 Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 44.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96RU2 (Residues: 149-399, 580-703; Coverage: 35%)
  • Best match: Q96RU2-3 (Residues: 149-399, 406-406)
Gene names: KIAA1515, USP28
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 78 amino acids
Theoretical weight: 8.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-227; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Unit cell:
a: 49.505Å b: 86.414Å c: 97.853Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.214
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli