6fge

X-ray diffraction
1.74Å resolution

Crystal structure of human ZUFSP/ZUP1 in complex with ubiquitin

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: 348 amino acids
Theoretical weight: 39.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96AP4 (Residues: 231-578; Coverage: 60%)
Gene names: C6orf113, ZUFSP, ZUP1
Sequence domains: Peptidase family C78
Ubiquitin Chain: C
Molecule details ›
Chain: C
Length: 76 amino acids
Theoretical weight: 8.56 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


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P6522
Unit cell:
a: 84.484Å b: 84.484Å c: 201.867Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.174 0.209
Expression system: Escherichia coli BL21(DE3)