PDBe 3ifw

X-ray diffraction
2.4Å resolution

Crystal structure of the S18Y variant of ubiquitin carboxy terminal hydrolase L1 bound to ubiquitin vinylmethylester.

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). 

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-683; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ubiquitin carboxyl-terminal hydrolase isozyme L1 Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 25.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09936 (Residues: 1-223; Coverage: 100%)
Gene name: UCHL1
Sequence domains: Ubiquitin carboxyl-terminal hydrolase, family 1
Structure domains: Ubiquitin C-terminal Hydrolase Uch-l3

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: R32
Unit cell:
a: 87.304Å b: 87.304Å c: 193.544Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.209 0.256
Expression system: Escherichia coli