5wwz

X-ray diffraction
2.5Å resolution

Crystal structure of the KH2 domain of human RNA-binding E3 ubiquitin-protein ligase MEX-3C

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-178346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding E3 ubiquitin-protein ligase MEX3C Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 86 amino acids
Theoretical weight: 9.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5U5Q3 (Residues: 320-396; Coverage: 12%)
Gene names: BM-013, MEX3C, RKHD2, RNF194
Sequence domains: KH domain
Structure domains: K Homology domain, type 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P42212
Unit cell:
a: 83.321Å b: 83.321Å c: 78.959Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.27
Expression system: Escherichia coli