› 8bd8

X-ray diffraction
3.1Å resolution

Crystal structure of TRIM33 alpha PHD-Bromo domain in complex with 8

Released:
DOI: 10.2210/pdb8bd8/pdb
PDB entry 8bd8 coloured by chain, front view.
PDB entry 8bd8 coloured by chain, side view.
PDB entry 8bd8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Exploiting ELIOT for Scaffold-Repurposing Opportunities: TRIM33 a Possible Novel E3 Ligase to Expand the Toolbox for PROTAC Design.
Palomba T, Tassone G, Vacca C, Bartalucci M, Valeri A, Pozzi C, Cross S, Siragusa L, Desantis J
Int J Mol Sci 23 (2022)
PMID: 36430693

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-194028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIM33 Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 24.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UPN9 (Residues: 882-1087; Coverage: 18%)
Gene names: KIAA1113, RFG7, TIF1G, TRIM33
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand QCU 1 x QCU
Ligand ZN 2 x ZN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P6522
Unit cell:
a: 80.015Å b: 80.015Å c: 134.469Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.21 0.338
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

PROTACs: A novel strategy for cancer drug discovery and development.
Han et al. (2023)
2 other articles

1 mention without citation

Exploiting ELIOT for Scaffold-Repurposing Opportunities: TRIM33 a Possible Novel E3 Ligase to Expand the Toolbox for PROTAC Design.
Palomba et al. (2022)