PDBe 2y5b

X-ray diffraction
2.7Å resolution

Structure of USP21 in complex with linear diubiquitin-aldehyde

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):
Ubiquitin carboxyl-terminal hydrolase 21 Chains: A, E
Molecule details ›
Chains: A, E
Length: 370 amino acids
Theoretical weight: 41.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UK80 (Residues: 196-565; Coverage: 66%)
Gene names: PP1490, USP21, USP23
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chains: B, F
Molecule details ›
Chains: B, F
Length: 152 amino acids
Theoretical weight: 17.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 77-228; Coverage: 66%)
Gene name: UBB
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 57.87Å b: 102.2Å c: 86.8Å
α: 90° β: 99.82° γ: 90°
R-values:
R R work R free
0.219 0.216 0.279
Expression system: Escherichia coli