› 2etl

X-ray diffraction
2.4Å resolution

Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)

Released:
DOI: 10.2210/pdb2etl/pdb
PDB entry 2etl coloured by chain, front view.
PDB entry 2etl coloured by chain, side view.
PDB entry 2etl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1.
Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA
Proc Natl Acad Sci U S A 103 4675-80 (2006)
PMID: 16537382

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-140823 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase isozyme L1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 25.27 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: Peptidase C12, ubiquitin carboxyl-terminal hydrolase

Ligands and Environments

1 bound ligand:
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P4212
Unit cell:
a: 110.097Å b: 110.097Å c: 79.489Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.223 0.274
Expression system: Escherichia coli

Quick links

Citations

29 review citations

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.
Reyes-Turcu et al. (2009)
28 more

25 mentions without citation

Regulation of proteolysis by human deubiquitinating enzymes.
Eletr et al. (2014)
24 more