PDBe 5o6c

X-ray diffraction
1.75Å resolution

Crystal Structure of a threonine-selective RCR E3 ligase

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase MYCBP2 Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75592 (Residues: 4417-4676; Coverage: 6%)
Gene names: KIAA0916, MYCBP2, PAM

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P61
Unit cell:
a: 82.578Å b: 82.578Å c: 103.303Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.172 0.196
Expression system: Escherichia coli