X-ray diffraction
1.85Å resolution

Catalytic fragment of UTX/KDM6A bound with N-oxyalylglycine, and Ni(II)

Source organism: Homo sapiens
Primary publication:
Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A.
Genes Dev. 25 2266-77 (2011)
PMID: 22002947

Function and Biology Details

Reaction catalysed:
(1a) a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(27) + 2-oxoglutarate + O(2) = a [histone H3]-N(6),N(6)-dimethyl-L-lysine(27) + succinate + formaldehyde + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Lysine-specific demethylase 6A Chain: A
Molecule details ›
Chain: A
Length: 531 amino acids
Theoretical weight: 60.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: O15550 (Residues: 880-1401; Coverage: 37%)
Gene names: KDM6A, UTX
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 78.872Å b: 82.879Å c: 92.923Å
α: 90° β: 90° γ: 90°
R R work R free
0.184 0.183 0.218
Expression system: Escherichia coli