PDBe 5kyc

X-ray diffraction
1.43Å resolution

Crystal structure of USP7 catalytic domain [V302K] mutant in complex with ubiquitin (malonate bound)

Released:
Source organism: Homo sapiens
Entry authors: Rouge L, Ozen A

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 7 Chain: B
Molecule details ›
Chain: B
Length: 351 amino acids
Theoretical weight: 40.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93009 (Residues: 208-554; Coverage: 32%)
Gene names: HAUSP, USP7
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chain: C
Molecule details ›
Chain: C
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 116.33Å b: 43.54Å c: 84.76Å
α: 90° β: 107.55° γ: 90°
R-values:
R R work R free
0.171 0.17 0.192
Expression system: Escherichia coli