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X-ray diffraction
2.15Å resolution

Crystal Structure of the S18Y Variant of Ubiquitin Carboxy-terminal Hydrolase L1

Released:
Source organism: Homo sapiens
Entry authors: Davies CW, Ringe D, Petsko GA, Das C

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:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
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: 25.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P4212
Unit cell:
a: 109.585Å b: 109.585Å c: 79.715Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.245
Expression system: Escherichia coli BL21