7ms7

X-ray diffraction
1.45Å resolution

Structure of USP5 zinc-finger ubiquitin binding domain co-crystallized with (5-((4-(4-chlorophenyl)piperidin-1-yl)sulfonyl)picolinoyl)glycine

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 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: 121 amino acids
Theoretical weight: 13.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45974 (Residues: 171-290; Coverage: 14%)
Gene names: ISOT, USP5
Sequence domains: Zn-finger in ubiquitin-hydrolases and other protein

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 61.556Å b: 84.87Å c: 59.542Å
α: 90° β: 98.86° γ: 90°
R-values:
R R work R free
0.17 0.169 0.181
Expression system: Escherichia coli