3lmn

X-ray diffraction
2.15Å resolution

Oligomeric structure of the DUSP domain of human USP15

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Asinas A, Avvakumov GV, Alenkin D, Weigelt J, Bountra C, Edwards AM, Arrowsmith CH, Bochkarev A, Dhe-Paganon S

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:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo octamer
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 15.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y4E8 (Residues: 1-133; Coverage: 14%)
Gene names: KIAA0529, USP15
Sequence domains: DUSP domain
Structure domains: DUSP-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: I4122
Unit cell:
a: 138.174Å b: 138.174Å c: 132.114Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.204
Expression system: Escherichia coli BL21(DE3)