PDBe 3lqi

X-ray diffraction
1.92Å resolution

Crystal structure of MLL1 PHD3-Bromo complexed with H3(1-9)K4me2 peptide

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
MLL cleavage product N320 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 183 amino acids
Theoretical weight: 21.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03164 (Residues: 1566-1784; Coverage: 5%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, TRX1
Sequence domains: PHD-finger
Structure domains:
Histone H3.1 Chains: R, S, T
Molecule details ›
Chains: R, S, T
Length: 9 amino acids
Theoretical weight: 1.09 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: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 48.744Å b: 90.584Å c: 125.085Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.241
Expression systems:
  • Escherichia coli
  • Not provided