› 6kcz

Solution NMR

Solution structure of the ZnF-UBP domain of USP20/VDU2

Released:
DOI: 10.2210/pdb6kcz/pdb
PDB entry 6kcz coloured by chain, ensemble of 20 models, front view.
PDB entry 6kcz coloured by chain, ensemble of 20 models, side view.
PDB entry 6kcz coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional studies of USP20 ZnF-UBP domain by NMR.
Yang Y, Ding Y, Zhou C, Wen Y, Zhang N
Protein Sci 28 1606-1619 (2019)
PMID: 31278784

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 20 Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y2K6 (Residues: 1-99; Coverage: 11%)
Gene names: KIAA1003, LSFR3A, USP20, VDU2
Sequence domains: Zn-finger in ubiquitin-hydrolases and other protein

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: simulated annealing
Expression system: Escherichia coli

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Citations

2 review citations

The emerging role of ubiquitin-specific protease 20 in tumorigenesis and cancer therapeutics.
Li et al. (2022)
1 more

1 mention without citation

Structural and functional studies of USP20 ZnF-UBP domain by NMR.
Yang et al. (2019)