› 3k2o

X-ray diffraction
1.75Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 39.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6NYC1 (Residues: 2-335; Coverage: 83%)
Gene names: JMJD6, KIAA0585, PSR, PTDSR
Sequence domains: JmjC domain, hydroxylase
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand NI 2 x NI
Ligand NA 2 x NA
Ligand CL 6 x CL
Ligand PO4 3 x PO4
Ligand ACT 2 x ACT
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 49.44Å b: 102.03Å c: 98.218Å
α: 90° β: 95.89° γ: 90°
R-values:
R R work R free
0.194 0.192 0.225
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein arginine methyltransferases and cancer.
Yang et al. (2013)
2 more

12 mentions without citation

Histone lysine methylation dynamics: establishment, regulation, and biological impact.
Black et al. (2012)
11 more