› 7r70

X-ray diffraction
2.5Å resolution

Crystal Structure of the UbArk2C fusion protein

Released:
DOI: 10.2210/pdb7r70/pdb
PDB entry 7r70 coloured by chain, front view.
PDB entry 7r70 coloured by chain, side view.
PDB entry 7r70 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C.
Paluda A, Middleton AJ, Rossig C, Mace PD, Day CL
OpenAccess logo Nat Commun 13 1181 (2022)
PMID: 35246518

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase ARK2C; Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG48 (Residues: 533-608; Coverage: 11%)
  • Canonical: Q6ZSG1 (Residues: 255-346; Coverage: 27%)
Gene names: ARK2C, RNF165, UBC
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P6222
Unit cell:
a: 154.47Å b: 154.47Å c: 81.706Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

From seeds to trees: how E2 enzymes grow ubiquitin chains.
Middleton et al. (2023)
4 other articles

1 mention without citation

Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C.
Paluda et al. (2022)