› 3lqh

X-ray diffraction
1.72Å resolution

Crystal structure of MLL1 PHD3-Bromo in the free form

Released:
DOI: 10.2210/pdb3lqh/pdb
PDB entry 3lqh coloured by chain, front view.
PDB entry 3lqh coloured by chain, side view.
PDB entry 3lqh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression.
Wang Z, Song J, Milne TA, Wang GG, Li H, Allis CD, Patel DJ
Cell 141 1183-94 (2010)
PMID: 20541251

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
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-169856 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MLL cleavage product N320 Chain: A
Molecule details ›
Chain: A
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:

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I222
Unit cell:
a: 63.219Å b: 71.879Å c: 93.867Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.234
Expression system: Escherichia coli

Quick links

Citations

57 review citations

The bromodomain interaction module.
Filippakopoulos et al. (2012)
56 more

8 mentions without citation

Readout of epigenetic modifications.
Patel et al. (2013)
7 more