PDBe 3vux

X-ray diffraction
1.7Å resolution

Crystal structure of A20 ZF7 in complex with linear ubiquitin, form II

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
A20p37 Chains: E, F, G
Molecule details ›
Chains: E, F, G
Length: 35 amino acids
Theoretical weight: 3.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21580 (Residues: 757-790; Coverage: 4%)
Gene names: OTUD7C, TNFAIP3
Sequence domains: A20-like zinc finger

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P31
Unit cell:
a: 62.329Å b: 62.329Å c: 85.18Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.165 0.203
Expression system: Escherichia coli