Solution NMR

Solution structure of MLL1 PHD3-Cyp33 RRM chimeric protein


Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
MLL cleavage product N320; Peptidyl-prolyl cis-trans isomerase E Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q03164 (Residues: 1585-1628; Coverage: 1%)
  • Canonical: Q9UNP9 (Residues: 2-82; Coverage: 27%)
Gene names: ALL1, CXXC7, CYP33, HRX, HTRX, KMT2A, MLL, MLL1, PPIE, TRX1
Sequence domains: RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli