Solution NMR

Solution NMR structure of the PHD domain of human MLL5, Northeast structural genomics consortium target HR6512A

Source organism: Homo sapiens
Entry authors: Lemak A, Yee A, Houliston S, Garcia M, Wu H, Min J, Montelione GT, Arrowsmith C, Northeast Structural Genomics Consortium (NESG), Structural Genomics Consortium (SGC), Chaperone-Enabled Studies of Epigenetic Regulation Enzymes (CEBS)

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Inactive histone-lysine N-methyltransferase 2E Chain: A
Molecule details ›
Chain: A
Length: 98 amino acids
Theoretical weight: 11.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q8IZD2 (Residues: 109-188; Coverage: 4%)
Gene names: KMT2E, MLL5
Sequence domains: PHD-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: restrained molecular dynamics
Chemical shifts: BMR18559  
Expression system: Escherichia coli