5ohk

X-ray diffraction
2.34Å resolution

Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (high resolution)

Released:
Source organism: Homo sapiens

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 30 Chain: A
Molecule details ›
Chain: A
Length: 336 amino acids
Theoretical weight: 38.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q70CQ3 (Residues: 64-178, 190-357, 432-502; Coverage: 63%)
Gene name: USP30
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.56 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: DIAMOND BEAMLINE I02
Unit cell:
a: 50.917Å b: 94.408Å c: 96.115Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.229 0.26
Expression system: Escherichia coli