› 3dkb

X-ray diffraction
2.5Å resolution

Crystal Structure of A20, 2.5 angstrom

Released:
DOI: 10.2210/pdb3dkb/pdb
PDB entry 3dkb coloured by chain, front view.
PDB entry 3dkb coloured by chain, side view.
PDB entry 3dkb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for the unique deubiquitinating activity of the NF-kappaB inhibitor A20.
Lin SC, Chung JY, Lamothe B, Rajashankar K, Lu M, Lo YC, Lam AY, Darnay BG, Wu H
J Mol Biol 376 526-40 (2008)
PMID: 18164316

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149309 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
A20p50 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 390 amino acids
Theoretical weight: 45.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21580 (Residues: 1-370; Coverage: 47%)
Gene names: OTUD7C, TNFAIP3
Sequence domains: OTU-like cysteine protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P32
Unit cell:
a: 123.636Å b: 123.636Å c: 143.043Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.246
Expression system: Escherichia coli

Quick links

Citations

47 review citations

The ubiquitin code.
Komander et al. (2012)
46 more

7 mentions without citation

Regulation of proteolysis by human deubiquitinating enzymes.
Eletr et al. (2014)
6 more