3zje

X-ray diffraction
1.84Å resolution

A20 OTU domain in reversibly oxidised (SOH) state

Released:

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
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
A20p50 Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 43.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P21580 (Residues: 1-366; Coverage: 46%)
Gene names: OTUD7C, TNFAIP3
Sequence domains: OTU-like cysteine protease

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 43.85Å b: 69.15Å c: 84.7Å
α: 99.14° β: 100.28° γ: 97.09°
R-values:
R R work R free
0.184 0.182 0.22
Expression system: Escherichia coli BL21