5lrx

X-ray diffraction
2.85Å resolution

Structure of A20 OTU domain bound to ubiquitin

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:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
A20p50 Chains: A, C
Molecule details ›
Chains: A, C
Length: 371 amino acids
Theoretical weight: 43.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21580 (Residues: 1-366; Coverage: 46%)
Gene names: OTUD7C, TNFAIP3
Sequence domains: OTU-like cysteine protease
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family
A20p50 Chains: E, F
Molecule details ›
Chains: E, F
Length: 371 amino acids
Theoretical weight: 43.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21580 (Residues: 1-366; Coverage: 46%)
Gene names: OTUD7C, TNFAIP3
Sequence domains: OTU-like cysteine protease

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 64.195Å b: 71.95Å c: 203.926Å
α: 90° β: 94.64° γ: 90°
R-values:
R R work R free
0.198 0.195 0.246
Expression system: Escherichia coli