6hek

X-ray diffraction
3.03Å resolution

Structure of human USP28 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 tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 28 Chains: A, C
Molecule details ›
Chains: A, C
Length: 556 amino acids
Theoretical weight: 64.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96RU2 (Residues: 149-703; Coverage: 52%)
Gene names: KIAA1515, USP28
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 78 amino acids
Theoretical weight: 8.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: I222
Unit cell:
a: 103.205Å b: 199.792Å c: 204.905Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.218 0.237
Expression system: Escherichia coli BL21(DE3)