3dkb

X-ray diffraction
2.5Å resolution

Crystal Structure of A20, 2.5 angstrom

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (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