PDBe 6ei1

X-ray diffraction
1.73Å resolution

Crystal structure of the covalent complex between deubiquitinase ZUFSP (ZUP1) and Ubiquitin-PA

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Zinc finger-containing ubiquitin peptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 347 amino acids
Theoretical weight: 39.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96AP4 (Residues: 232-578; Coverage: 60%)
Gene names: C6orf113, ZUFSP, ZUP1
Sequence domains: Peptidase family C78
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG47 (Residues: 153-227; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P6522
Unit cell:
a: 84.23Å b: 84.23Å c: 201.78Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.171 0.203
Expression system: Escherichia coli BL21(DE3)