› 3qzv

X-ray diffraction
2Å resolution

Crystal Structure of BPTF PHD-linker-bromo in complex with histone H4K12ac peptide

Released:
DOI: 10.2210/pdb3qzv/pdb
PDB entry 3qzv coloured by chain, front view.
PDB entry 3qzv coloured by chain, side view.
PDB entry 3qzv coloured by chain, top view.
Source organisms:
Primary publication:
Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions.
Ruthenburg AJ, Li H, Milne TA, Dewell S, McGinty RK, Yuen M, Ueberheide B, Dou Y, Muir TW, Patel DJ, Allis CD
Cell 145 692-706 (2011)
PMID: 21596426

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158677 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nucleosome-remodeling factor subunit BPTF Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 20.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12830 (Residues: 2865-3033; Coverage: 6%)
Gene names: BPTF, FAC1, FALZ
Sequence domains:
Structure domains:
Histone H4 Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.07 KDa
Source organism: Xenopus laevis
Expression system: Not provided
UniProt:
  • Canonical: P62805 (Residues: 8-18; Coverage: 11%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 65.525Å b: 38.513Å c: 87.752Å
α: 90° β: 111.2° γ: 90°
R-values:
R R work R free
0.186 0.182 0.234
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

82 review citations

Cancer epigenetics: from mechanism to therapy.
Dawson et al. (2012)
81 more

4 mentions without citation

Writers and readers of histone acetylation: structure, mechanism, and inhibition.
Marmorstein et al. (2014)
3 more