› 3pua

X-ray diffraction
1.89Å resolution

PHF2 Jumonji-NOG-Ni(II)

Released:
DOI: 10.2210/pdb3pua/pdb
PDB entry 3pua coloured by chain, front view.
PDB entry 3pua coloured by chain, side view.
PDB entry 3pua 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 Chain: A
Molecule details ›
Chain: A
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

4 bound ligands:
Ligand NI 1 x NI
Ligand EDO 11 x EDO
Ligand CL 1 x CL
Ligand OGA 1 x OGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 109.575Å b: 65.767Å c: 66.612Å
α: 90° β: 102.09° γ: 90°
R-values:
R R work R free
0.167 0.164 0.21
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

6 mentions without citation

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