3wxe

X-ray diffraction
2.5Å resolution

Crystal structure of CYLD USP domain (C596S) in complex with Met1-linked diubiquitin

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).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-123083 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase CYLD Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 35.99 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: E7FEV5 (Residues: 578-780, 850-951; Coverage: 32%)
Gene name: cylda
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: Cysteine proteinases
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 148 amino acids
Theoretical weight: 16.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 533-680; Coverage: 22%)
Gene name: UBC
Sequence domains: Ubiquitin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 64.676Å b: 49.788Å c: 71.003Å
α: 90° β: 102.69° γ: 90°
R-values:
R R work R free
0.185 0.182 0.247
Expression system: Escherichia coli