PDBe 1whm

Solution NMR

Solution structure of the 2nd CAP-Gly domain in human cylindromatosis tumor suppressor CYLD

Released:
Source organism: Homo sapiens
Entry authors: Saitok K, Koshiba S, Inoue M, Kigawa T, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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: 92 amino acids
Theoretical weight: 9.57 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9NQC7 (Residues: 228-304; Coverage: 8%)
  • Best match: Q9NQC7-2 (Residues: 228-306)
Gene names: CYLD, CYLD1, HSPC057, KIAA0849
Structure domains: CAP Gly-rich-like domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

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