5k1b

X-ray diffraction
3.3Å resolution

Crystal structure of the UAF1/USP12 complex in F222 space group

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).

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-130890 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
WD repeat-containing protein 48 Chain: B
Molecule details ›
Chain: B
Length: 677 amino acids
Theoretical weight: 76.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q8TAF3 (Residues: 1-677; Coverage: 100%)
Gene names: KIAA1449, UAF1, WDR48
Sequence domains:
Ubiquitin carboxyl-terminal hydrolase 12 Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 42.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: O75317 (Residues: 4-370; Coverage: 99%)
Gene names: UBH1, USP12, USP12L1
Sequence domains: Ubiquitin carboxyl-terminal hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: F222
Unit cell:
a: 120.958Å b: 158.929Å c: 234.584Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.235 0.286
Expression system: Escherichia coli K-12