2miq

Solution NMR

Solution NMR Structure of PHD Type 1 Zinc Finger Domain 1 of Lysine-specific Demethylase Lid from Drosophila melanogaster, Northeast Structural Genomics Consortium (NESG) Target FR824J

Released:
Source organism: Drosophila melanogaster
Entry authors: Xu X, Eletsky A, Shastry R, Maglaqui M, Janjua H, Xiao R, Everett JK, Sukumaran DK, Montelione GT, Szyperski T, Northeast Structural Genomics Consortium (NESG), Chaperone-Enabled Studies of Epigenetic Regulation Enzymes (CEBS)

Function and Biology Details

Reaction catalysed:
(1a) a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(4) + 2-oxoglutarate + O(2) = a [histone H3]-N(6),N(6)-dimethyl-L-lysine(4) + succinate + formaldehyde + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-194280 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine-specific demethylase 5 Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 10.1 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9VMJ7 (Residues: 414-504; Coverage: 5%)
Gene names: CG9088, Kdm5, lid
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: simulated annealing
Expression system: Escherichia coli BL21(DE3)