3emh

X-ray diffraction
1.37Å resolution

Structural basis of WDR5-MLL interaction

Released:
Source organism: Homo sapiens
Primary publication:
WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket.
J. Biol. Chem. 283 35258-64 (2008)
PMID: 18840606

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
WD repeat-containing protein 5 Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 34.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61964 (Residues: 25-334; Coverage: 93%)
Gene names: BIG3, WDR5
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
MLL cleavage product C180 Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.5 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q03164 (Residues: 3764-3776; Coverage: 0%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, TRX1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 78.44Å b: 98.29Å c: 80.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.2
Expression systems:
  • Escherichia coli
  • Not provided