4pqt

X-ray diffraction
2.05Å resolution

Insights into the mechanism of deubiquitination by JAMM deubiquitinases from co-crystal structures of enzyme with substrate and product

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
AMSH-like protease sst2 Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 21.94 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P371 (Residues: 245-435; Coverage: 44%)
Gene names: SPAC19B12.10, sst2
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Structure domains: Cytidine Deaminase, domain 2
Protein UBBP4 Chain: B
Molecule details ›
Chain: B
Length: 81 amino acids
Theoretical weight: 8.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 42.413Å b: 58.003Å c: 56.189Å
α: 90° β: 108.97° γ: 90°
R-values:
R R work R free
0.204 0.202 0.252
Expression system: Escherichia coli