4m3l

X-ray diffraction
2.1Å resolution

Crystal Structure of the coiled coil domain of MuRF1

Released:

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-188340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIM63 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 61 amino acids
Theoretical weight: 7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q969Q1 (Residues: 214-271; Coverage: 16%)
Gene names: IRF, MURF1, RNF28, SMRZ, TRIM63
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 70.79Å b: 24.41Å c: 75.39Å
α: 90° β: 107.65° γ: 90°
R-values:
R R work R free
0.214 0.212 0.262
Expression system: Escherichia coli