5fzo

X-ray diffraction
1.84Å resolution

Crystal structure of the catalytic domain of human JmjD1C

Released:
Source organism: Homo sapiens
Entry authors: Nowak R, Talon R, Krojer T, Goubin S, McDonough M, Fairhead M, Oppermann U, Johansson C

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-172367 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Probable JmjC domain-containing histone demethylation protein 2C Chain: A
Molecule details ›
Chain: A
Length: 352 amino acids
Theoretical weight: 40.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15652 (Residues: 2157-2500; Coverage: 14%)
Gene names: JHDM2C, JMJD1C, KIAA1380, TRIP8
Sequence domains: JmjC domain, hydroxylase
Structure domains: Cupin
Probable JmjC domain-containing histone demethylation protein 2C Chain: B
Molecule details ›
Chain: B
Length: 352 amino acids
Theoretical weight: 40.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15652 (Residues: 2157-2500; Coverage: 14%)
Gene names: JHDM2C, JMJD1C, KIAA1380, TRIP8
Sequence domains: JmjC domain, hydroxylase
Structure domains: Cupin

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Unit cell:
a: 45.32Å b: 110.92Å c: 165.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.231
Expression system: Escherichia coli BL21(DE3)