2uzg

Solution NMR

Zf-UBP domain of VDU1

Released:
Source organism: Homo sapiens
Primary publication:
The solution structure of the ZnF UBP domain of USP33/VDU1.
Protein Sci 16 2072-5 (2007)
PMID: 17766394

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
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-186261 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 33 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8TEY7 (Residues: 36-130; Coverage: 10%)
Gene names: KIAA1097, USP33, VDU1
Sequence domains: Zn-finger in ubiquitin-hydrolases and other protein
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: CNS
Expression system: Escherichia coli BL21(DE3)