2ysm

Solution NMR

Solution structure of the second and third PHD domain from Histone-lysine N-methyltransferase 2C (KMT2C/MLL3)

Released:
Source organism: Homo sapiens
Entry authors: Qin XR, Hayashi F, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase 2C Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: cell-free protein synthesis
UniProt:
  • Canonical: Q8NEZ4 (Residues: 342-439; Coverage: 2%)
Gene names: HALR, KIAA1506, KMT2C, MLL3
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: 94%
Refinement method: torsion angle dynamics
Chemical shifts: BMR11237  
Expression system: cell-free protein synthesis