3ihr

X-ray diffraction
2.95Å resolution

Crystal Structure of Uch37

Released:
Source organism: Homo sapiens
Primary publication:
Structural characterization of human Uch37.
Proteins 80 649-54 (2012)
PMID: 21953935

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:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-195276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase isozyme L5 Chain: A
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 37.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y5K5 (Residues: 1-329; Coverage: 100%)
Gene names: AD-019, CGI-70, UCH37, UCHL5
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: I222
Unit cell:
a: 90.092Å b: 98.736Å c: 154.061Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.242
Expression system: Escherichia coli