PDBe 5ohn

X-ray diffraction
3.6Å resolution

Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (low 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 Chains: A, C
Molecule details ›
Chains: A, C
Length: 370 amino acids
Theoretical weight: 42.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q70CQ3 (Residues: 64-357, 432-502; Coverage: 71%)
Gene name: USP30
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P65
Unit cell:
a: 181.834Å b: 181.834Å c: 94.957Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.211 0.253
Expression system: Escherichia coli BL21(DE3)