PDBe 1ixd

Solution NMR

Solution structure of the CAP-GLY domain from human cylindromatosis tomour-suppressor CYLD

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 Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 10.87 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9NQC7 (Residues: 460-550; Coverage: 10%)
Gene names: CYLD, CYLD1, HSPC057, KIAA0849
Sequence domains: CAP-Gly domain
Structure domains: SH3 type barrels.

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Not provided