PDBe 3nhe

X-ray diffraction
1.26Å resolution

High Resolution Structure (1.26A) of USP2a in Complex with Ubiquitin

Released:
Source organism: Homo sapiens
Entry authors: Schormann N, DeLucas LJ, Powell McCombs D

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 2 Chain: A
Molecule details ›
Chain: A
Length: 348 amino acids
Theoretical weight: 40.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75604 (Residues: 258-605; Coverage: 58%)
Gene names: UBP41, USP2
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: Cysteine proteinases
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62979 (Residues: 1-76; Coverage: 49%)
Gene names: RPS27A, UBA80, UBCEP1
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 102.771Å b: 53.961Å c: 74.719Å
α: 90° β: 107.71° γ: 90°
R-values:
R R work R free
0.17 0.169 0.189
Expression system: Escherichia coli BL21(DE3)