PDBe 2vhf

X-ray diffraction
2.8Å resolution

Structure of the CYLD USP domain

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).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase CYLD Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 43.35 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9NQC7 (Residues: 583-956; Coverage: 39%)
Gene names: CYLD, CYLD1, HSPC057, KIAA0849
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 60.494Å b: 89.083Å c: 171.806Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.233 0.281
Expression system: Spodoptera frugiperda