› 2rje

X-ray diffraction
1.86Å resolution

Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), orthorhombic form II

Released:
DOI: 10.2210/pdb2rje/pdb
PDB entry 2rje coloured by chain, front view.
PDB entry 2rje coloured by chain, side view.
PDB entry 2rje coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
L3MBTL1 recognition of mono- and dimethylated histones.
Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, MacKenzie F, Vedadi M, Arrowsmith CH
Nat Struct Mol Biol 14 1229-30 (2007)
PMID: 18026117

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-158691 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lethal(3)malignant brain tumor-like protein 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 331 amino acids
Theoretical weight: 37.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y468 (Residues: 268-598; Coverage: 39%)
Gene names: KIAA0681, L3MBT, L3MBTL, L3MBTL1
Sequence domains: mbt repeat
Structure domains: SH3 type barrels.
Histone H4 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 11 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62805 (Residues: 16-26; Coverage: 11%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
1 modified residue:
Ligand MLY 2 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P21212
Unit cell:
a: 109.894Å b: 124.64Å c: 90.031Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.231
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

57 review citations

Double-strand break repair: 53BP1 comes into focus.
Panier et al. (2014)
56 more

1 mention without citation

The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression.
West et al. (2010)