› 6kqv

Solution NMR

Solution Structure of the UbL Domain of USP19

Released:
DOI: 10.2210/pdb6kqv/pdb
PDB entry 6kqv coloured by chain, ensemble of 10 models, front view.
PDB entry 6kqv coloured by chain, ensemble of 10 models, side view.
PDB entry 6kqv coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Domain interactions reveal auto-inhibition of the deubiquitinating enzyme USP19 and its activation by HSP90 in the modulation of huntingtin aggregation.
Xue W, Zhang SX, He WT, Hong JY, Jiang LL, Hu HY
Biochem J 477 4295-4312 (2020)
PMID: 33094816

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 19 Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94966 (Residues: 679-766; Coverage: 7%)
Gene names: KIAA0891, USP19, ZMYND9

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 66%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Emerging Role of Ubiquitin-Specific Protease 19 in Oncogenesis and Cancer Development.
Rossi et al. (2022)
1 other article