5d0i

X-ray diffraction
1.9Å resolution

Structure of RING finger protein 165

Released:
Source organism: Homo sapiens
Primary publication:
Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity.
Nat Struct Mol Biol 23 45-52 (2016)
PMID: 26656854

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-180599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase ARK2C Chains: A, B
Molecule details ›
Chains: A, B
Length: 97 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6ZSG1 (Residues: 255-346; Coverage: 27%)
Gene names: ARK2C, RNF165
Sequence domains: Ring finger domain
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P43212
Unit cell:
a: 76.22Å b: 76.22Å c: 103.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.2
Expression system: Escherichia coli