› 3o7a

X-ray diffraction
1.67Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183268 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
PHD finger protein 13 Chain: A
Molecule details ›
Chain: A
Length: 52 amino acids
Theoretical weight: 6.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86YI8 (Residues: 229-280; Coverage: 17%)
Gene name: PHF13
Sequence domains: PhD finger domain
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
Histone H3 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.29 KDa
Source organism: Xenopus laevis
Expression system: Not provided
UniProt:
  • Canonical: Q92133 (Residues: 2-12; Coverage: 8%)
Gene names: H3l, Hist1h3f, h3, h3.2a, h3c8, h3c8.S, h3r, hist1h3g, hist1h3g.L, hist2h3, hist2h3c

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand ZN 2 x ZN
1 modified residue:
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 21.232Å b: 44.334Å c: 60.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.224
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Is H3K4me3 instructive for transcription activation?
Howe et al. (2017)
4 more

5 mentions without citation

Solution NMR structure and histone binding of the PHD domain of human MLL5.
Lemak et al. (2013)
4 more