2dak

Solution NMR

Solution Structure of the Second UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)

Released:
Source organism: Homo sapiens
Entry authors: Zhao C, Kigawa T, Sato M, Koshiba S, Inoue M, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-155377 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 5 Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 6.52 KDa
Source organism: Homo sapiens
Expression system: Cell free synthesis
UniProt:
  • Canonical: P45974 (Residues: 723-772; Coverage: 6%)
Gene names: ISOT, USP5
Sequence domains: UBA/TS-N domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, restrainted molecular dynamics
Expression system: Cell free synthesis