› 3a7s

X-ray diffraction
2.2Å resolution

Catalytic domain of UCH37

Released:
DOI: 10.2210/pdb3a7s/pdb
PDB entry 3a7s coloured by chain, front view.
PDB entry 3a7s coloured by chain, side view.
PDB entry 3a7s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain.
Nishio K, Kim SW, Kawai K, Mizushima T, Yamane T, Hamazaki J, Murata S, Tanaka K, Morimoto Y
Biochem Biophys Res Commun 390 855-60 (2009)
PMID: 19836345

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 analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-195274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase isozyme L5 Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 25.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5K5 (Residues: 1-228; Coverage: 69%)
Gene names: AD-019, CGI-70, UCH37, UCHL5
Sequence domains: Ubiquitin carboxyl-terminal hydrolase, family 1
Structure domains: Peptidase C12, ubiquitin carboxyl-terminal hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 67.583Å b: 57.064Å c: 48.736Å
α: 90° β: 100.91° γ: 90°
R-values:
R R work R free
0.205 0.205 0.255
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Mechanisms of Deubiquitinase Specificity and Regulation.
Mevissen et al. (2017)
7 more

6 mentions without citation

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