2l80

Solution NMR

Solution Structure of the Zinc Finger Domain of USP13

Released:
Source organism: Homo sapiens
Entry authors: Zhang Y, Zhou C, Zhou Z, Song A, Hu H

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-187829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 13 Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 12.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92995 (Residues: 188-301; Coverage: 13%)
Gene names: ISOT3, USP13
Sequence domains: Zn-finger in ubiquitin-hydrolases and other protein
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)