5jjw

X-ray diffraction
3.01Å resolution

Crystal structure of the HAT domain of sart3 in complex with USP15 DUSP-UBL domain

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zhang Q, Walker JR, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, 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).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Squamous cell carcinoma antigen recognized by T-cells 3 Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 35.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15020 (Residues: 280-578; Coverage: 31%)
Gene names: KIAA0156, SART3, TIP110
Ubiquitin carboxyl-terminal hydrolase 15 Chain: B
Molecule details ›
Chain: B
Length: 224 amino acids
Theoretical weight: 26.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y4E8 (Residues: 1-223; Coverage: 23%)
Gene names: KIAA0529, USP15
Sequence domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6422
Unit cell:
a: 117.925Å b: 117.925Å c: 205.326Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.234 0.288
Expression system: Escherichia coli