X-ray diffraction
1.79Å resolution

Crystal structure of WDR5 in complex with the WDR5-interacting motif of SET1A


Function and Biology Details

Reaction catalysed:
(1a) 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:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
WD repeat-containing protein 5 Chains: A, C
Molecule details ›
Chains: A, C
Length: 318 amino acids
Theoretical weight: 34.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • 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 SETD1A Chains: B, D
Molecule details ›
Chains: B, D
Length: 11 amino acids
Theoretical weight: 1.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: O15047 (Residues: 1492-1502; Coverage: 1%)
Gene names: KIAA0339, KMT2F, SET1, SET1A, SETD1A

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: P21
Unit cell:
a: 64.89Å b: 47.1Å c: 102.52Å
α: 90° β: 108.21° γ: 90°
R R work R free
0.195 0.194 0.23
Expression systems:
  • Escherichia coli
  • Not provided