PDBe 1cmx

X-ray diffraction
2.25Å resolution

STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase YUH1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 235 amino acids
Theoretical weight: 26.28 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P35127 (Residues: 1-235; Coverage: 100%)
Gene names: J1941, YJR099W, YUH1
Sequence domains: Ubiquitin carboxyl-terminal hydrolase, family 1
Structure domains: Ubiquitin C-terminal Hydrolase Uch-l3
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: R3
Unit cell:
a: 199.3Å b: 199.3Å c: 36.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.248 0.248 0.285
Expression system: Not provided