› 3pus

X-ray diffraction
2.08Å resolution

PHF2 Jumonji-NOG-Ni(II)

Released:
DOI: 10.2210/pdb3pus/pdb
PDB entry 3pus coloured by chain, front view.
PDB entry 3pus coloured by chain, side view.
PDB entry 3pus coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for human PHF2 Jumonji domain interaction with metal ions.
Horton JR, Upadhyay AK, Hashimoto H, Zhang X, Cheng X
J Mol Biol 406 1-8 (2011)
PMID: 21167174

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine-specific demethylase PHF2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 44.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75151 (Residues: 60-451; Coverage: 36%)
Gene names: CENP-35, KIAA0662, PHF2
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand EDO 14 x EDO
Ligand CL 2 x CL
Ligand NI 2 x NI
Ligand OGA 2 x OGA
Ligand OXY 1 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 65.353Å b: 96.979Å c: 66.194Å
α: 90° β: 89.78° γ: 90°
R-values:
R R work R free
0.177 0.175 0.232
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Histone lysine demethylases as targets for anticancer therapy.
Højfeldt et al. (2013)
10 more

4 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
3 more