PDBe 3u5p

X-ray diffraction
2.8Å resolution

Crystal structure of the complex of TRIM33 PHD-Bromo and H3(1-28)K9me3K14acK18acK23ac histone peptide

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase TRIM33 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 207 amino acids
Theoretical weight: 23.83 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:
Structure domains:
Histone H3.1 Chains: I, J, K, L, M, N, O, P
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 28 amino acids
Theoretical weight: 3.17 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-29; Coverage: 21%)
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:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 63.426Å b: 63.608Å c: 124.611Å
α: 90.01° β: 90.04° γ: 90°
R-values:
R R work R free
0.213 0.21 0.265
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided