PDBe 5mr8

X-ray diffraction
1.74Å resolution

Crystal structure of TRIM33 PHD-Bromodomain isoform B in complex with H3K9ac histone peptide

Released:
Source organism: Homo sapiens
Entry authors: Tallant C, Savitsky P, Fedorov O, Nunez-Alonso G, Siejka P, Krojer T, Williams E, Srikannathasan V, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Muller S, Knapp S, Structural Genomics Consortium (SGC)

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase TRIM33 Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 22.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UPN9 (Residues: 882-1090; Coverage: 17%)
  • Best match: Q9UPN9-2 (Residues: 882-1073)
Gene names: KIAA1113, RFG7, TIF1G, TRIM33
Sequence domains: PHD-finger
Histone H3.1 Chain: C
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 1.1 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-10; Coverage: 7%)
Gene names: H3FA, H3FB, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 50.885Å b: 57.994Å c: 71.488Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.286
Expression systems:
  • Escherichia coli
  • Not provided