› 3uvm

X-ray diffraction
1.57Å resolution

Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4

Released:
DOI: 10.2210/pdb3uvm/pdb
PDB entry 3uvm coloured by chain, front view.
PDB entry 3uvm coloured by chain, side view.
PDB entry 3uvm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.
Zhang P, Lee H, Brunzelle JS, Couture JF
Nucleic Acids Res 40 4237-46 (2012)
PMID: 22266653

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158502 (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: 34.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61964 (Residues: 21-334; Coverage: 94%)
Gene names: BIG3, WDR5
Sequence domains: WD domain, G-beta repeat
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Histone-lysine N-methyltransferase 2B Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.11 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UMN6 (Residues: 2508-2517; Coverage: 0%)
Gene names: HRX2, KIAA0304, KMT2B, MLL2, MLL4, TRX2, WBP7

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: C2221
Unit cell:
a: 78.527Å b: 98.774Å c: 79.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.198
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

23 review citations

Hijacked in cancer: the KMT2 (MLL) family of methyltransferases.
Rao et al. (2015)
22 more

2 mentions without citation

The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.
Zhang et al. (2012)
1 more