› 6heh

X-ray diffraction
2.26Å resolution

Structure of the catalytic domain of USP28 (insertion deleted)

Released:
DOI: 10.2210/pdb6heh/pdb
PDB entry 6heh coloured by chain, front view.
PDB entry 6heh coloured by chain, side view.
PDB entry 6heh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity.
Gersch M, Wagstaff JL, Toms AV, Graves B, Freund SMV, Komander D
Mol Cell 74 436-451.e7 (2019)
PMID: 30926242

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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%)
Gene names: KIAA1515, USP28
Sequence domains: Ubiquitin carboxyl-terminal hydrolase

Ligands and Environments

2 bound ligands:
Ligand EDO 1 x EDO
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: I4132
Unit cell:
a: 189.152Å b: 189.152Å c: 189.152Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Deubiquitylases in developmental ubiquitin signaling and congenital diseases.
Basar et al. (2021)
11 more

1 mention without citation

Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity.
Gersch et al. (2019)