PDBe 5fwi

X-ray diffraction
3.4Å resolution

structure of usp7 catalytic domain and three ubl-domains

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).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 7 Chain: C
Molecule details ›
Chain: C
Length: 680 amino acids
Theoretical weight: 78.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q93009 (Residues: 207-882; Coverage: 61%)
Gene names: HAUSP, USP7
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: F222
Unit cell:
a: 115.183Å b: 195.04Å c: 219.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.267
Expression system: Escherichia coli BL21