2g43

X-ray diffraction
2.09Å resolution

Structure of the ZNF UBP domain from deubiquitinating enzyme isopeptidase T (IsoT)

Released:

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-155377 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 14.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45974 (Residues: 163-291; Coverage: 15%)
Gene names: ISOT, USP5
Sequence domains: Zn-finger in ubiquitin-hydrolases and other protein
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C, null
Spacegroup: C2
Unit cell:
a: 61.38Å b: 86.18Å c: 59.9Å
α: 90° β: 99.29° γ: 90°
R-values:
R R work R free
0.228 0.228 0.274
Expression system: Escherichia coli