› 3tb3

X-ray diffraction
2.3Å resolution

Crystal structure of the UCH domain of UCH-L5 with 6 residues deleted

Released:
DOI: 10.2210/pdb3tb3/pdb
PDB entry 3tb3 coloured by chain, front view.
PDB entry 3tb3 coloured by chain, side view.
PDB entry 3tb3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains.
Zhou ZR, Zhang YH, Liu S, Song AX, Hu HY
Biochem J 441 143-9 (2012)
PMID: 21851340

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase isozyme L5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 25.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5K5 (Residues: 1-227; 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 CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 47.54Å b: 102.34Å c: 47.06Å
α: 90° β: 92.13° γ: 90°
R-values:
R R work R free
0.223 0.222 0.269
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Deubiquitylases from genes to organism.
Clague et al. (2013)
11 more