› 2vfj

X-ray diffraction
3.2Å resolution

Structure of the A20 Ovarian Tumour (OTU) domain

Released:
DOI: 10.2210/pdb2vfj/pdb
PDB entry 2vfj coloured by chain, front view.
PDB entry 2vfj coloured by chain, side view.
PDB entry 2vfj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the A20 OTU domain and mechanistic insights into deubiquitination.
Komander D, Barford D
Biochem J 409 77-85 (2008)
PMID: 17961127

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
Molecule details ›
Chains: A, B, C, D
Length: 366 amino acids
Theoretical weight: 43.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21580 (Residues: 1-366; Coverage: 46%)
Gene names: OTUD7C, TNFAIP3
Sequence domains: OTU-like cysteine protease

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 84.964Å b: 83.023Å c: 164.94Å
α: 90° β: 98.08° γ: 90°
R-values:
R R work R free
0.206 0.204 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

44 review citations

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

11 mentions without citation

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