3ppa

X-ray diffraction
2.35Å resolution

Structure of the Dusp-Ubl domains of Usp15

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Asinas AE, Dong A, Weigelt J, Bountra C, Edwards AM, Arrowsmith CH, Dhe-Paganon S, Structural Genomics Consortium (SGC)

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

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 15 Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 27.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y4E8 (Residues: 6-223; Coverage: 22%)
Gene names: KIAA0529, USP15
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6222
Unit cell:
a: 74.17Å b: 74.17Å c: 194.52Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.263 0.262 0.285
Expression system: Escherichia coli BL21(DE3)