› 6k2k

Solution NMR

Solution structure of MUL1-RING domain

Released:
DOI: 10.2210/pdb6k2k/pdb
PDB entry 6k2k coloured by chain, ensemble of 20 models, front view.
PDB entry 6k2k coloured by chain, ensemble of 20 models, side view.
PDB entry 6k2k coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of MUL1-RING domain and its interaction with p53 transactivation domain.
Lee MS, Lee SO, Lee MK, Yi GS, Lee CK, Ryu KS, Chi SW
Biochem Biophys Res Commun 516 533-539 (2019)
PMID: 31235254

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial ubiquitin ligase activator of NFKB 1 Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q969V5 (Residues: 297-352; Coverage: 16%)
Gene names: C1orf166, GIDE, MAPL, MUL1, MULAN, RNF218
Sequence domains: Zinc finger, C3HC4 type (RING finger)

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 review citations

On the specificity of protein-protein interactions in the context of disorder.
Teilum et al. (2021)
3 more

2 mentions without citation

The RING domain of mitochondrial E3 ubiquitin ligase 1 and its complex with Ube2D2: crystallization and X-ray diffraction.
Lee et al. (2020)
1 more