› 2rhu

X-ray diffraction
1.9Å resolution

Crystal structure of the 3-MBT repeats from human L3MBTL1 bound to dimethyl-lysine and in chimera with histone H3.3(28-34)

Released:
DOI: 10.2210/pdb2rhu/pdb
PDB entry 2rhu coloured by chain, front view.
PDB entry 2rhu coloured by chain, side view.
PDB entry 2rhu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger.
Li H, Fischle W, Wang W, Duncan EM, Liang L, Murakami-Ishibe S, Allis CD, Patel DJ
Mol Cell 28 677-91 (2007)
PMID: 18042461

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lethal(3)malignant brain tumor-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 37.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y468 (Residues: 274-587, 592-598; Coverage: 38%)
Gene names: KIAA0681, L3MBT, L3MBTL, L3MBTL1
Sequence domains: mbt repeat
Structure domains: SH3 type barrels.

Ligands and Environments

4 bound ligands:
Ligand SO4 1 x SO4
Ligand MLY 1 x MLY
Ligand PG4 1 x PG4
Ligand PEG 1 x PEG
1 modified residue:
Ligand CML 2 x CML

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 85.166Å b: 94.023Å c: 59.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.215
Expression system: Escherichia coli

Quick links

Citations

54 review citations

Histones: annotating chromatin.
Campos et al. (2009)
53 more

1 mention without citation

Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger.
Li et al. (2007)