› 2muu

Solution NMR

The Proteolytic Activity of Ubiquitin-specific Protease 28 Is Modulated by the N-terminal Domain

Released:
DOI: 10.2210/pdb2muu/pdb
PDB entry 2muu coloured by chain, ensemble of 14 models, front view.
PDB entry 2muu coloured by chain, ensemble of 14 models, side view.
PDB entry 2muu coloured by chain, ensemble of 14 models, top view.
Source organism: Homo sapiens
Primary publication:
The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
Wen Y, Shi L, Ding Y, Cui R, He WT, Hu HY, Zhang N
Biochem J 471 155-65 (2015)
PMID: 26268556

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
Sequence domain:

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: 137 amino acids
Theoretical weight: 14.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96RU2 (Residues: 1-120; Coverage: 11%)
Gene names: KIAA1515, USP28

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Ubiquitin-specific protease 28: the decipherment of its dual roles in cancer development.
Ren et al. (2023)
3 other articles